臺灣博碩士論文加值系統

本博士論文主要在探討無花果乳汁β-N-乙醯胺基六碳糖苷酶 (β-NAHA) 和綠竹筍幾丁聚醣酶之生化學性質，並以綠竹筍幾丁聚醣酶製備低分子量幾丁聚醣 後，評估其安全性及對腎損傷小鼠之影響。研究分四部分進行：第一部分，由無花果乳汁分離一主要之β-NAHA，探討其生化性質包括分子量、等電點、熱穩定性、活性影響物質和基質專一性以及混合基質動力學，結果顯示無花果乳汁β-NAHA對β-醣苷鍵具專一性，水解p-nitrophenyl-N-acetyl-β-D-glucosaminide和p-nitrophenyl-N-acetyl--D-galactosaminide二基質係屬同一活性中心。第二部分，將新鮮採收之綠竹筍經由幾丁聚醣誘發後，分離、純化幾丁聚醣酶，並探討其生化特性，結果顯示純化之綠竹筍幾丁聚醣酶分子量為12.7 kDa；其可水解不同程度去乙醯度 (10.9-94%) 幾丁聚醣，其中對30% 去乙醯度之幾丁聚醣具有最高活性。第三部分以綠竹筍幾丁聚醣酶降解幾丁聚醣製備分子量約29 kDa之低分子量幾丁聚醣；經動物試驗安全性評估結果顯示，研究所得之低分子量幾丁聚醣不會造成細胞核損傷，亦不具急毒性及亞急毒性，其無毒性劑量超過1g/kg BW。第四部份，以馬兜鈴酸誘發小鼠產生腎損傷，探討餵食低分子量幾丁聚醣對小鼠腎損傷之修護作用。經生化學及組織病理切片分析結果顯示，連續14天給予中劑量500 mg/kg BW/day之低分子量幾丁聚醣可有效改善馬兜鈴酸所誘發之腎損傷。

This dissertation aimed to investigate the biochemical properties of β-N-acetylhexosaminidase (β-NAHA) from fig latex and chitosanase from bamboo shoots, as well as the safety evaluation and effect of low molecular weight chitosan (LMWC), prepared by bamboo chitosanase, on mice with renal lesions. Four studies were conducted to reach the goals of researches. First, a major β-NAHA was purified from fig latex. Biochemical properties, including molecular mass, isoelectric point, thermal stability, effectors, and substrate specificity, of the purified β-NAHA and kinetics of competition for the enzyme with mixed substrates were studied. The results indicated that the activity of the fig β-NAHA was specific for the β-glycoside linkage, and the enzyme had only one active site for binding both substrates p-nitrophenyl-N-acetyl-β-D-glucosaminide and p-nitrophenyl-N-acetyl-β-D-galactosaminide. In the second part of study, a predominant chitosanase induced by chitosan was isolated and purified from edible bamboo shoots. The biochemical properties of the purified chitosanase were studied as well. The results indicated that the molecular mass of the purified chitosanase was 12.7 kDa, and this enzyme was capable of hydrolyzing chitosan polymers with various degree of deacetylation (10.9-94%) and the chitosan with ~30% deacetyled was the most susceptible. In the third part of study, a LMWC (~29 kDa) was prepared by the depolymerzation of chitosan using partially purified bamboo chitosanase. Animal experiments showed that the LMWC did not cause damage of nucleus in mice and had no toxicity in rats, and the no-observed-adverse-effect level (NOAEL) was greater than 1 g/kgBW in rats. In the fourth part of study, renal lesions were induced by aristolochic acid (AA) in mice and then the repairing effect of LMWC on renal lesions was studied. The results of biochemical analysis and histophathological examination indicated that oral administration of LMWC at a middle dose of 500 mg/kg BW/day for 14 days effectively ameliorated AA-induced renal lesions in mice.

目 錄

誌 謝 I
目 錄 II
表目錄 VIII
圖目錄 IX
縮寫表 XI

中文摘要 1
Abstract 3
前 言 5

第一部分 11
中文摘要 (第一部分) 13
Abstract (part I) 14
第一章 前言 15
第二章 文獻回顧 17
第一節β-NAHA之生理功能 17
第二節β-NAHA之分佈 17
壹、微生物 17
貳、動物 17
參、植物 18
第三節 β-NAHA之理化性質 18
壹、一般生化性質 18
貳、基質特異性 18
參、活性影響物質 19
第四節 pH值對酵素催化活性之影響 20
第五節 β-NAHA作用機制 21
第六節 β-NAHA的胺基酸與醣類之組成 24
第七節 研究動機與目的 24
第三章 材料與方法 25
第一節 實驗材料 25
壹、無花果乳汁 25
貳、化學藥品 25
第二節 實驗方法 26
壹、pAPMA-Sepharose 親和吸著劑製備 26
貳、幾丁質酶活性測定 30
參、幾丁聚醣酶活性測定 30
肆、β-NAHA活性測定 30
伍、醣苷水解酵素活性測定 30
陸、蛋白酶活性測定 31
柒、β-NAHA之純化 31
捌、β-NAHA性質測定 32
玖、蛋白質定量 37
拾 活性中心測定方法 38
第四章 結果與討論 39
第一節 無花果乳汁之蛋白酶、幾丁聚合物水解酵素及糖苷水解酵素活性 39
第二節 pAPMA-Sepharose親和吸著劑之製備 39
第三節 β-NAHA之純化 40
第四節β-NAHA之性質 46
壹、最適pH及pH穩定性: 46
貳、最適溫度及熱穩定性. 46
參、動力學參數Km及最大反應速率 (Vmax) 49
肆、分子量 52
伍、等電點 55
陸、活性影響物質 57
柒、基質專一性 60
捌、反應活化能 61
第五章 結論 63

第二部分 65
中文摘要 (第二部分) 67
Abstract (Part II) 68
第一章 前言 69
第二章 文獻回顧 71
第一節 幾丁質與幾丁聚醣 71
壹、幾丁質 71
貳、幾丁聚醣 71
第二節 幾丁聚醣酶 72
壹、微生物幾丁聚醣酶 72
貳、動物幾丁聚醣酶 74
參、植物幾丁聚醣酶 74
第三節 幾丁聚醣酶之活性測定及應用 79
壹、幾丁聚醣酶的活性測定 79
貳、幾丁聚醣酶之應用 79
第四節 研究動機與目的 79
第三章 材料與方法 80
第一節 實驗材料 80
壹、綠竹筍 (Bambusa oldhamii) 80
貳、化學藥品 80
第二節 重要器材及儀器 80
第三節 實驗方法 81
壹、綠竹筍採收後之幾丁聚醣處理 81
貳、還原糖校正曲線製作 82
參、幾丁聚醣酶活性測定 82
肆、幾丁聚醣酶的純化 82
伍、幾丁聚醣酶的性質測定 84
陸、蛋白質定量 88
第四章 結果與討論 90
第一節 native-PAGE電泳及幾丁聚醣酶活性染色 90
第二節 幾丁聚醣酶純化 92
第三節 幾丁聚醣酶性質 98
壹、最適pH： 98
貳、最適溫度： 99
參、熱穩定性： 100
肆、不同去乙醯度幾丁聚醣對酵素活性之影響 101
伍、分子量 102
陸、等電點 105
柒、SDS-PAGE及酵素活性染色 108
捌、金屬離子對酵素活性之影響： 109
第五章 結論 110

第三部分 111
中文摘要 (第三部分) 113
Abstract (Part III) 115
第一章 前言 117
第二章 文獻回顧 119
第一節 幾丁聚醣(Chitosan)之生理功能 119
第二節 LMWC及COS之製備 119
第三節 幾丁聚醣水解產物之新穎生理功能 120
第四節 食品安全性評估分類 121
第五節 微核試驗 (Micronuclues test) 123
壹、微核試驗的目的與意義..…..…. 123
貳、微核試驗原理 123
參、Acridine orange (A.O.)螢光染色 124
第六節 單一劑量口服毒性試驗 (Acute oral toxicity limit test) 124
壹、單一劑量口服毒性試驗的目的 124
貳、單一劑量口服毒性試驗的評估方法 125
第七節 28天餵食毒性試驗 (28-day feeding toxicity study) 126
壹、28天餵食毒性試驗的目的 126
貳、28天餵食毒性試驗的評估方法 126
第八節 研究動機與目的 127
第三章 材料與方法 128
第一節 酵素法製備水溶性低分子量幾丁聚醣 128
壹、實驗材料 128
貳、實驗方法 128
第二節 LMWC之安全性評估 132
壹、實驗材料 132
貳、實驗方法 133
第四章 結果與討論 137
第一節 幾丁聚醣水解產物製備 137
壹、不同水解時間甲醇區分水解產物之回收率 137
貳、不同水解時間所得LMWC產物之膠體過濾層析 137
參、LMWC-A之MBTH呈色定量分析 144
肆、LMWC-A之溶解度 144
第二節 LMWC之安全性評估 146
壹、微核試驗 146
貳、單一劑量口服毒性試驗 (Acute oral toxicity limit test) 150
參、28天餵食毒性試驗 (28-day feeding toxicity study) 156
第五章 結論 162

第四部分 163
中文摘要 (第四部分) 165
Abstract (Part IV) 166
第一章 前言 167
第二章 文獻回顧 170
第一節 馬兜鈴酸與腎病變 170
壹、腎臟生理與功能 170
貳、馬兜鈴酸腎病變流行病學 170
參、馬兜鈴酸基本特性 171
肆、馬兜鈴酸腎毒性 172
伍、幾丁聚醣之改善腎損傷功效 174
第二節 研究動機與目的 174
第三章 材料與方法 175
第一節 實驗材料 175
壹、實驗動物 175
貳、化學藥品 175
参、管餵樣品 175
肆、儀器器材 175
第二節 實驗方法 176
壹、動物飼養條件 176
貳、飼料配方 176
參、樣品劑量 176
肆、動物實驗過程 176
伍、體重測量 179
陸、血樣收集 179
柒、尿液收集 179
捌、實驗動物生化值之測定方法 180
玖、統計分析 184
拾、動物犧牲組織切片製作及Periodic Acid Schiff’s stain (PAS)組織 染色、hematoxylin and eosin (H&E)和Masson's trichrome (TRI) 三種組織染色 184
拾壹、腎組織損傷程度的量化 184
第四章 結果與討論 185
第一節 餵食LMWC對AA誘發腎損傷小鼠之影響 185
壹、小鼠體重 185
貳、尿液中微白蛋白 (microalbumin) 186
參、尿中總蛋白 189
肆、尿液NAG酵素活性 192
伍、血清中肌酸酐 195
陸、肌酸酐廓清率 (Ccr) 198
柒、血液尿素氮 201
捌、馬兜鈴酸誘發腎損傷過程之腎組織病理PAS染色 203
玖、馬兜鈴酸誘發腎損傷過程之腎組織損傷量化分析 206
拾、攝取LMWC後腎組織修護之病理H&E染色 207
拾壹、TRI染色 209
拾貳、攝取LMWC後腎組織損傷修護量化分析 210
第五章 結論 212

結 論 213
未來展望 214
參考文獻 215

任澤銀、龔慧、丁敬韜、唐志利 (2004) 馬兜鈴酸引起腎臟損害的臨床觀察。中國醫師雜誌。6:1283-1284。
曲明、劉丹 (2005) 防己與廣防己的鑒別。中醫藥信息。22:36-37。
江翠蓮、張珍田 (2006) 無花果蛋白酶酵素製品之幾丁質酶性質研究。台灣農業化學與食品科學，44: 207-215。
行政院衛生署(1999) 健康食品管理法。台北。
吳杰、陳香美、師鎖柱（2005）急慢性馬兜鈴酸腎病的臨床病理特點及其病理機制。 中華檢驗醫學雜誌。28:587-590.
吳冠政（2006） 纖維素酶水解幾丁聚醣及其產物免疫活性評估。國立台灣海洋大學食品科學研究所博士論文。基隆市，台灣。
李宗明 (2003) 綠竹筍幾丁質酶之純化與生化性質研究。國立台灣大學農業化學研究所碩士論文。台北市，台灣。
李瑛、劉志紅、郭嘯華、蘇健、陳朝紅、周虹、黎磊石（2004）馬兜鈴酸Ⅰ致腎小管上皮細胞DNA損傷的實驗研究。腎臟定與透析腎臟移植雜誌。13:6-12。
林秀錦 (1998) 蘿蔔與蕪菁根部 β-N-乙醯胺基六碳醣苷酶之純化及性質研究。靜宜大學食品營養學系碩士論文。台中市，台灣。
林翰良 (1995) 以固定化幾丁聚醣酶生產幾丁聚醣水解物及其抗菌之研究。東海大學食品科學研究所碩士論文。台中市，台灣。
徐叔雲 (1982) 藥理實驗方法學，人民衛生出版社，北京。
張婷雅 (2005) 馬兜鈴酸腎症在純系小鼠的確立與綠茶、(+)-catechin和pravastatin sodium在此腎炎模型的藥效評估。台北醫學大學藥學研究所碩士論文。台北市，台灣。
張粲如 (1993) 綠竹筍採收後生理與保鮮技術。作物之遺傳育種及生理栽培研討會專輯。pp. 123-140。
黃怡雯 (2001) 以纖維素酶水解幾丁聚醣所得之水溶性產物對腸內細菌組成之影響。國立台灣海洋大學食品科學研究所碩士論文。基隆市，台灣。
楊文淇 (2005) 馬兜鈴酸腎症在純系小鼠的確立與柴胡在此腎炎模型的藥效評估。台北醫學大學藥學系碩士論文。台北市，台灣。
葉貞妤 (2003) 綠竹筍外殼幾丁聚醣酶之純化及性質研究。靜宜大學食品營養學系碩士論文。台中市，台灣。
詹社紅 (2002) 探討寡木糖的攝取對成年大白鼠腸道生理及菌叢影響。靜宜大學食品營養研究所碩士論文。台中市，台灣。
詹淑玲 (2001) 低分子幾丁聚醣與幾丁寡醣對大鼠腸道菌群及生理之影響。國立台灣海洋大學食品科學研究所碩士論文。基隆市，台灣。
廖倍瑜 (2004) 木瓜酵素粗製品之基丁聚合物水解酵素研究。靜宜大學食品營養研究所碩士論文。台中市，台灣。
廖倍瑜、吳佩甄、江翠蓮、張珍田 (2006) 木瓜乳汁乾燥製品之幾丁質酶及幾丁聚醣酶研究。台灣農業化學與食品科學，44: 217-227。
蔡少青、王璇、張翠英、李曉玫、李彪（2004）馬兜鈴酸Ⅰ及馬兜鈴內酰胺Ⅰ對腎小管上皮細胞損傷的差異。北京大學學報(醫學版)。36: 36-40。
蔡培芳 (2003) 綠竹筍cDNA之選殖與檢定。國立台灣大學農業化學研究所碩士論文。台北市，台灣。
蔡國珍，吳冠政，詹淑玲 (2002) 幾丁寡醣之抗菌及免疫活性。2002年幾丁質幾丁聚醣研討會論專輯，中華幾丁質幾丁聚醣學會，基隆市，pp. S43-S45.
鄭法霞、蘇震 (2002) 慢性馬兜鈴酸腎病的研究發展，中國中西醫結合腎病雜誌。3: 313-316。
顏國欽 (1989) 食品安全學。藝軒出版社。台北市，台灣。
Agrawal, K. M. L. and Bahl, O. P. (1968) Glycosidases of Phaseolusvulgaris. II. Isolatinon and general properoties. J. Biol. Chem. 243:103-111.
Agrawal, K. M. L. and Bahl, O. P. (1972) -galactosidase, -galactosidase, -glucosidase, -N-acetylglucosaminidase, and -mannosidase from pinto beans (Phaseolus rulgaris) In Methods in Enzymology, (Colowick, S.P. and Kaplan, N. O. Eds) Vol. 28, pp. 720-728, Academic Press, New York.
Akiyama, K., Kawazu, K. and Kobayashi, A. (1995) A novel method for chemo-enzymatic synthesis of elicitor-active chitosan oligomers and partially N-deacetylated chitin oligomers using N-acetylated chitotrioses as substrates in a lysozyme-catalyzed transglycosylation reaction system. Carbohydr. Res. 279(27): 151-160.
Allan, G. G. and Peyron, M. (1995a) Molecular weight manipulation of chitosan. I: Kinetics of depolymerization by nitrous acid. Carbohydr. Res. 277: 257-272.
Allan, G. G. and Peyron, M. (1995b) Molecular weight manipulation of chitosan. I: Kinetics of depolymerization by nitrous acid. Carbohydr. Res. 277: 273-282.
Andrews, P. (1965) The gel-filtration behavior of proteins related to their molecular weights over a wide range. Biochem. J. 96: 596-606.
Anson, M. L. (1939) The estimation of pepsin, trypsin, papain and cathepsin with hemoglobin. J. Gen. Physiol. 22: 79-89.
Araki, Y. and Ito, E. (1975) A pathway of chitosan formation in Mucor muxii, enzymatic deacetylation of chitin. Eur. Biochem. 55: 71-78.
Arlt, V. M., Stiborova, M. and Schmeiser, H. H. (2002) Aristolochic acid as a probable human cancer hazard in herbal remedies: a review. Mutagenesis. 17: 265-277.
Aruchami, M., Gowri, N. and Rajulu, G. S. (1982) Detection and characterization of chitosanase from termites. In Chitin and Chitosan (Hirano, S., Tokura, S. Eds) The Japanese Society of Chitin and Chitosan Publication, Sapporo, Japan, pp. 131-134.
Arvanitoyannis, I. S., Nakayama, A. and Aiba, S. (1998) Chitosan and gelatin based edible films: state diagrams, mechanical and permeation properties. Carbohydrate. Polymers. 37: 371-382.
Austin, P. R., Brine, C. T., Castle, J. E. and Zikakis, J. P. (1981) Chitin: New facets of research. Science. 212 (5): 749-753.
Avadi, M. R., Sadeghi, A. M. M., Rahzibi, A., Bayati, Kh., Pouladzadeh, M., Zohuriaan-Mebr, M. J. and Rafiee-Tehrani, M. (2004) Diethylmethyl chitosan as an antimicrobial agent: symthesis, characterization and antibacterial effects. Eur. Polym. J. 40: 1355-1361.
Bahl, O. P . and Agrawal, K. M. L. (1969) Glycosidase of Aspergillusniger : Ⅰ. Purification and characterization of α- and β-galactosidase and β-N-acetyl-glucosaminidase. J. Biol. Chem. 244: 2970-2978.
Bahl, O. P. and Agrawal, K. M. L. (1968) Glycosidases of Phaseolusvulgaris.I. Isolation and characterization of β -N-acetylglucosaminidase. J. Biol. Chem. 243: 98-102.
Ballantyne, B., Marrs, T. and Syversen, T. (1999). General and Applied Toxicology. Vol. 3. Bath Press. Ballantyn.
Barber, M. S. and Ride, J. P. (1989) Purification and properties of a wheat leaf N-acetyl--D-hexosaminidase. Plant Sci. 60: 163-172.
Bartnicki-Garcia, S. (1968) Cell wall chemistry, morphogenesis and taxonomy of fungi. In Annu. Rev. Microbiol. 22: 87-108.
Bazzi, C., Petrini, C., Rizza, V., Arrigo, G., Napodano, P., Paparella, M. and D'Amico, G. (2002) Urinary N-acetyl-beta-glucosaminidase excretion is a marker of tubular cell dysfunction and a predictor of outcome in primary glomerulonephritis. Nephnol. Dial. Transplant. 17: 1890-1896.
Bedi, G. S., Shah, R. H. and Bahl, O. P. (1984a) Studies on Turbatrixaceti ß-N-acetylglucosaminidase purification and physiochemical characterization. Arch. Biochem. Biophy. 233: 237-250.
Bedi, G. S., Shah, R. H. and Bahl, O. P. (1984b) Studies on Turbatrixaceti β-N-acetylglucosaminidase Kinetic studies on the active site. Arch. Biochem. Biophy. 233: 251-259.
Blackwell, J. and Weik, W. A. (1984) The structure of chitin-protein complexes. In Chitin, Chitosan and Relates Enzymes (Zikzkis, J. P. Ed.), Academic Press, New York. pp. 257-272
Boller, T. and Kende, H. (1979) Hydrolytic enzymes in the central vacuole of plant cell. Plant Physiol. 63: 1123-1132.
Boller, T., Gehri, A., Manch, F. and Vogeli, B. U. (1983) Chitinase in bean leaves : induction by ethylene, purification, properties, and possible fuction. Planta. 157: 22-31.
Boller, T., Gehri, A., Manch, F. and Vogeli, B. U. (1983) Chitinase in bean leaves : induction by ethylene, purification, properties, and possible fuction. Planta. 157: 22-31.
Bosomworth, M. P., Aparicio, S. R. and Hay, A. W. (1999) Urine N-acetyl-beta-D-glucosaminidase--a marker of tubular damage? Nephnol. Dial. Transplant. 14: 620-626.
Boucher, I., Dupuy, A., Vidal, P., Neugebauer, W. A. and Brzezinski, R. (1992) Purification and characterization of a chitosanase from Streptomyces N174. Appl. Microbiol. Biotechnol. 38: 188-193.
Bouquelent, S. and Spik, G. (1976) Characterization and location of fourform of N-acetyl-β-D-hexosaminidase form renugreek germinated seed. FEBS Letters 63: 95-101.
Bourbouze, R., Baumann, F. C., Bonvalet, J. P. and Farman N. (1984) Distribution of N-acetyl-beta-D-glucosaminidase isoenzymes along the rabbit nephron. Kidney Int. 25: 636-642.
Bourdeau, J. E. and Carone, F. A. (1974) Protein handling by the renal tubule. Nephron. 13: 22-34.
Boyer, P. D. (1954) Spectrophotometric study of the reaction of the proteins sulfhydryl groups with organic mercurials. J. Am. Chem. Soc. 76: 4331-4337.
Bradford, M. M. (1976) A rapid and sensitive method for the quantization of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72: 248-254.
Broekaert, W. J., Lee, H. I., Kush, A., Chua, N. H. and Raikhel, N. V. (1990) Proc. Natl. Acad. USA, 87: 7633-7637 .
Burton, C. J. and Walls, J. (1996) Interstitial inflammation and scarring: messages from the proximal tubular cell. Nephnol. Dial. Transplant. 11: 1505-1507.
Cabib, E. (1987) The synthesis and degradation of chitin. In Advance Enzymology. 59: 84-86.
Calvo, P., Reglero, A. and Cabezas, J. A. (1978) Purification and properties of -N-acetylhexosaminidase from the molluse Helicella evicetrorum Muller. Biochem. J. 175: 743-750.
Carraty, G., Colacino, C., Conti, S. and Giannattasid, M. (1985) β-N-acetylglucosaminidase and β -galactosidase from aleurone layers of resting wheat grains. Phytochemisity. 24: 1465-1469.
Chang, C. T., Young, F. P., Chang, M. H. and Sung, H.Y. (1998) Purification and properties of β-N-acetylhexosaminidase from cabbage. Biochem. Mol. Biol. Int. 45: 371-380.
Chen, C. S., liau, W. Y. and Tsai, G. J. (1998) Antibacterial effects of N-sulfonated and sulfobenzoyl chitosan and application to oyster preservation. J. Food. Prot. 61(9): 1124-1130.
Chen, Y.-C., Liu, W.-L., Hsu, H.-C., Lee, Y.-A. and Chen, C.-S. (2004) Purification and characterization of isoforms of β-N-acetylhexosaminidase from mungbean seedlings. Bot. Bull. Acad. Sin. 45: 275-283.
Chiang, C. L., Chang, Y. M., Chang, C. T. and Sung, H. Y. (2005) Characterization of a chitosanase isolated from a commercial ficin preparation. J. Agric. Food Chem. 53: 7579-7585.
Choi, S. Y. and Gross, K. C. (1994) N-acetyl β-D-glucosaminidase from｀golden delicious＇apples. Phytochemisity. 36: 1-6.
Chye, M. L. and Cheung, K. Y. (1995) ß-1,3-glucanase is highly expresses in laticifers of Hevea brasiliensis. Plant Mol. Biol. 29: 397-402.
Cody R. M. (1989) Distribution of chitinase and chitobiase in Bacillus. Curr. Microbiol. 19: 201-205.
Collinge, D. B. and Kragh, K. M. (1993) Plant chitinase. Plant J. 3: 31-40.
Conrath, U., Domard, A. and Kauss, H. (1989) Chitosan-elicited synthesis of callose and of coumarin derivatives in parsley cell suspension cultures. Plant Cell Rep. 8: 152-155.
Cosyns, J. P, Goebbels, R. M., Liberton, V., Schmeiser, H. H., Bieler, C. A. and Bernard, A. M. (1998) Chinese herbs nephropathy-associated slimming regimen induces tumors in the fore stomach but no interstitial nephropathy in rats. Arch. Toxicol. 72: 738-743.
Cosyns J-P (2003) Aristolochic acid and 'Chinese herbs nephropathy': a review of the evidence to date. Drug Safety. 26:33-48.
Cosyns, J. P. (2002) When is "aristolochic acid nephropathy" more accurate than "Chinese herbs nephropathy"?[comment]. Kidney Int. 61:1178.
Cosyns, J. P., Dehoux, J. P., Guiot, Y., Goebbels, R. M., Robert, A., Bernard, A. M. and van Ypersele de Strihou, C. (2001) Chronic aristolochic acid toxicity in rabbits: a model of Chinese herbs nephropathy [see comment]. Kidney Int. 59: 2164-2173.
Cosyns, J. P., Jadoul, M., Squifflet, J. P., Cangh, P. J. and van Ypersele de Strihou, C. (1994b) Urothelial malignancy in nephropathy due to Chinese herbs. Lancet. 344:188.
Cosyns, J. P., Jadoul, M., Squifflet, J. P., De Plaen, J. F., Ferluga, D. and Ypersele de Strihou, C. (1994a) Chinese herbs nephropathy: a clue to Balkan endemic nephropathy? Kidney Int. 45: 1680-1688.
Counahan, R., Chantler, C., Ghazali, S., Kirkwood, B., Rose, F. and Barratt, T. M. (1976) Estimation of glomerular filtration rate from plasma creatinine concentration in children. Arch. Dis. Child. 51: 875-878.
Cuatrecasas, P. (1970) Protein purification by affinity chromatography. J. Biol. Chem. 245: 3059-3065.
Cuero, R. G. (1999) Antimicrbial action of exogenous. In Chitin and Chitosan (Jolles, P. and Muzzarelli, R. A-A. Eds.) Birkhauser verlag Basel/Swetzerland, pp. 315-333.
Cuero, R. G. (1999) Antimicrobial action of exogenous chitosan. In Chitin and Chitosan (Jolles, P. and Muzzarelli, R. A. A. Eds.) Birkhauser Verlag Basel Swtzerland, pp. 315-333.
Cuero, R. G. and Osuji, G. (1991) Chitosanase bioinduction by two strains of Bacillus sp. and chitosan in peanut: an effective biocontrol of pathogenic and toxigenic fungi. Med. Fac. Landbouww. Rijksuniv. Gent , 56 (4a): 1415-1425.
Cuero, R. G. and Osuji, G. O. (1993) Chitosanase induction in maize and peanuts: enzyme induction factors. In Chitin Enzymology (Muzzarelli, R. A. A. Ed.) Eur. Chitin Soc., Amcona, pp. 277-282.
Cuero, R. G., Waniska, R., Fajardo, J., Osuji, G. and Duffus, E. (1992) Enhancement of phytoalexin and chitosanase by chitosan in germinating peanuts, biocontrol of toxigenic fungi and myzotoxins. In Advanced Chitin and Chitosan (Brine, C. J., Sandford, P. A. and Eikakis, J. J. Eds), Elsevier, London, pp. 419-432.
Datema, R., Wessels, J. G. H. and Van Den Ende, H. (1977) The hyphal wall of Mucor mucedo. Z. Hexosamine-containing polymers. Eur. J. Biochem. 80:621-626.
Davis, B. J. (1964) Disc electrophoresis-II. Method and application to human serum proteins. Ann. N. Y. Acad. Sci. 121: 404-427.
Dawson, R. M. C., Elliott, D. C., Elliott, W. H. and Jones, K. M. (1969) Data for Biochemical Research, pp. 483-498, Oxford, Clarendon.
De Jong, A. J., Cordewener, J., Schiavo, F. L., Terzi, M., Vandekerckhove, J., Kammen, A. V. and De Vries, S. C. (1992) A carrot somatic embryo mutant is rescued by chitinase. Plant Cell. 4: 425-433.
Debelle, F. D., Nortier, J. L., De Prez, E. G., Garbar, C. H., Vienne, A. R., Salmon, I. J., Deschodt-Lanckman, M. M. and Vanherweghem, J. L. (2002) Aristolochic acids induce chronic renal failure with interstitial fibrosis in salt-depleted rats. J. Am. Soc. Nephrol. 13: 431-436.
Depierreux, M., Van Damme, B., Vanden Houte, K. and Vanherweghem, J. L. (1994) Pathologic aspects of a newly described nephropathy related to the prolonged use of Chinese herbs. Am. J. Kidney Dis. 24: 172-180.
Deuchi, K., Kanauchi, O., Imasato, Y. and Kobayashi, E. (1994) Decreasing effect of chitosan on the apparent fat digestibility by rats fed on a high-fat diet. Biosci. Biotech. Biochem. 58: 1613-1616.
Dixon, M., Webb, E. C., Thorne, C. R. and Tipton, K. F. (1979) Enzyme.3rd Ed, Longman Group Ltd. London.
Domard, A. and Cartier, N. (1989) Glucosamine oligomers I. Preparation and Characterization. Int. J. Biol. Marcromol. 11: 297-302.
Dubois, M., Gilles, K. A., Hamilton, J. K., Reers, P. A and Smith, F. (1956) Colorimetric method for determination of sugars and related substances. Anal. Chem. 28: 350-356.
Dumas-Gaudot, E., Grenier, J., Furlan, V. and Asselin, A. (1992) Chitinase, chitosanase and -1, 3 glucanase activities in Allium and Pisam roots colonized by Glomus species. Plant Sci. 84: 17-24.
Dygert, S., Li, L. H., Florida, D. and Thoma, J. A. (1965) Determination of reducing sugar with improved precision. Anal. Biochem. 13:367-374.
Eastmond, D. A. and Tucker, J. D. (1989). Identification of aneuploidy-inducing agents using cytokinesis-blocked human lymphocytes and an antikinetochore antibody. Environ. Mol. Mutag. 13(1) : 34-43.
Eddy, A. A. (2000) Molecular basis of renal fibrosis. Pediatr Nephrol. 15: 290-301.
EI-Ghaouth, A., Amilanick, J. L. and Wilson, C. L. (2000) Enhancement of the performance of Candida saitoana by the addition of glycol chitosan for the control of postharvest decay of apple and citrus fruit. Postharvest Biol. Techmol. 19: 103-110.
EI-Ghaouth, A., Arul, J. and Asselin, A. (1992a) A potential use of chitosan in postharvest preservation of fruits and vegetables. In Advances in Chitin and Chitosan (Brines, J. B., Sanford, O. A. and Zilalis, J. P. Eds) Elsevier Applied Sci., London, pp. 440-452.
El Ghaouth, A., Arul, J. Asselin, A. and Benhamou, N. (1992b) Antifungal activity of chitosan on two post-harvest pathogens of strawberry fruits. Phytopathology 82: 398-402.
Fajardo, J. E., Waniska, R. D., Cuero, R. G. and Pittit, R. E. (1995) Phenolic compounds in peanut seeds : Enhanced elicitation by chitosan and effects on growth and aflatoxin B1 production by Aspergillus flavus. Food Technol. 9 (182): 59-78.
Fenech, M., Holland, N., Chang, W. P., Zeiger, E., and Bonassi, S. (1999). The Human MicroNucleus project - an international collaborative study on the use of the micronucleus technique for measuring DNA damage in humans. Mutation Research-Fundamental and Molecular Mechanisms of Mutagenesis, 428 (1-2) :271-283.
Fenton, D. M. and Eveleigh, D. E. (1981) Purification and mode of action of a chitosanase from Penicillium islandium. J. Gen. Microbiol. 126: 151-165.
Fenton, D., Davis, B., Rotgers, C. and Eveleigh, D. E. (1978) Enzymic hydrolysis of chitosan. In Proc. First International Conf. on Chitin/Chitosan (Muzzarell, R. A. A. and Pariser, E. R. Eds), MIT Press, Cambridge, MA, pp.525-534.
Finco, D. R., Brown, S. A., Vaden, S. L. and Ferguson, D. C. (1995) Relationship between plasma creatinine concentration and glomerular filtration rate in dogs. J. Veter. Pharm. Therap. 18: 418-421.
Flach, J., Pilt, P. E. and Jollr, P. (1992) What’s new in chitinase research ? Experieta. 48: 701-716.
Fu, J. Y., Wu, S. M., Chang, C. T. and Sung, H. Y. (2003) Characterization of three chitosanase isozymes isolated from a commercial crude porcine pepsin preparation. J. Agric. Food Chem. 51: 1042-1048.
Gao, R., Zheng, F., Liu, Y., Zheng, D., Li, X., Bo, Y. and Liu, Y. (2000) Aristolochic acid I-induced apoptosis in LLC-PK1 cells and amelioration of the apoptotic damage by calcium antagonist. Chinese Med. J. 113: 418-424.
Gers-Barlag, H., Bartz, I. and Ruoiger, H. (1988) β-N-acetylhexosaminidase from soybean. Phytochemistry. 27: 3739-3741.
Giordani, R. and Noat, G. (1988) Isolation, molecular properties and kinetics studies of a strict -fucosidase from Lactuca sativa latex. Its possible role in the cell-wall degradation of the articulated laticifers. Eur. J. Biochem. 175: 619-625.
Giordani, R., Benyahia, S., Teissere, M. and Noat, G. (1992) Purification and properties of β-N-acetylglucosaminidase from Heveabrasilliensis latex. Plant Sci. 84(12): 25-34.
Giustina, A. and Ventura, P. (1995) Weight-reducing regimens in obese subjects: effects of a new dietary fiber integrator. Acta. Toxicol Ther. 16:199-214.
Glasgow, L. R., Paulson, J. C. and Hill, R. L. (1977) Systematic purification of five glycosidase from Streptococcus (Diplococcus) pneumoniae. J. Biol. Chem. 252: 8615-8623.
Glazer, A. M. and Faraney, D. (1969) Sulfonyl fluoride as inhibitor of esterase. Ⅱ Formation and reactions of phenylmethylsulfonyl α-chymotrypsin. Biochemistry. 3: 783-791.
Gold, A. M. and Fahrney, D. E. (1964) Sulfonyl fluorides as inhibitors of esterases. II Formation and reactions of phenylmethane sulfonyl α-chymotrypsin. Biochemistry. 3: 783-791.
Graham, L. S. and Sticklen, M. B. (1994) Plant chitinases, Can. J. Bot. 72: 1057-1083.
Grenier, J. and Asselin, A. (1990) Some pathogenesis related proteins are chitosanase with lytic activity against fungal spores. Mol. Plant. Microb. Interact. 3: 401-407.
Grenier, J., Benhamon, N. and Asselin, A. (1991) Colloidal gold-complexed chitosanase: a new probe for ultrastructural localization of chitosan in fungi. J. Gen. Microbiol. 137: 2007-2015.
Hadwiger, L. A., Fristensky, B. and Riggleman, R. C. (1984) Chitosan a natural regulator in plant-fungal pathogen, increases crop yields. In Chitin, Chitosan and Related Enzymes (Zikakis, J. P. Ed.), Academic Press, Orlando, pp. 291-320.
Hamel, R., Boivin, R., Tremblay, C. and Bellemare, G. (1997) Structural and evolutionary relationships among chitinase of flowering plants. J. Mol. Evol. 44: 614-624.
Harley, S. M. and Beevers, L. (1987) Isozymes of -N-acetylhexosaminidase from pea seeds (Pisum sativum L.) Plant Physiol. 85: 1118-1122.
Hasega, M., Yagi, K., Iwakawa, S. and Hirai, M. (2001) Chitosan induces apoptosis via caspase-3 activation in bladder tumor cells. Jpn. J. Cancer Res. P2: 459-466.
Hatakey, K., Hiramatus, M. and Minami, N. (1980) Reduction of N-acetylglucosaminidase activity in the submaxillary glands of streptozotocin diabetic mice. Biochem. J. 88: 613-615.
Hayashi, M., Sofuni, T. and Ishidate Jr, M. (1983). An application of acridine orange fluorescent staining to the micronuclear test. Mutat. Res. 120(4): 241-247.
Helander, I. M., Nurmiaho-Lassila, E.-L., Ahvenainen, R., Rhoades, J. and Roller, S. (2001) Chitosan disrupts the barrier properties of the outer membrane of Gram-negative bacteria. Int. J. Food Microbiol. 71: 235-244.
Hirano, S., Yamamoto, T., Hayashi, M., Nishida, T. and Inui, H. (1990) Chitinase activity in seeds coated with chitosan derivates. Agric. Biol. Chem. 54: 2719-2720.
Hodge, A. Alexander, I. J. and Gooday, G. W. (1996) Measurement in situ of chitinase and β-N-acetyl-glucosaminidase activities in germinating seeds of Pinus sylvestris and Eucalyptus pilularis. Plant Physiol. Biochem. 34: 301-307.
Hofmeister, R., Bhargava, A. S. and Gunzel, P. (1990) The use of uninary N-acetyl-β-D-glucosaminidase (NAG) for the detection of contrast-Media-induced｀osmotic nephrosis＇in rat. Toxicol. Lett. 50: 9-15.
Holmes, G. J. and Eckert, J. W. (1999) Sensitivity of Penicillium digitatum and P. italicum to postharvest citrus fungicides in California, Phytopathology 89: 716-721.
Horowite, S. T., Rouseman, S. and Blumenthal, H. J. (1957) The preparation of glucosamine oligosaccharides I. Separation. J. Am. Chem. Soc. 79: 5064-5049.
Hrabar, A., Ceovic, S., Aleraj, B., Cvoriscec, D. and Hall, P. W. 3rd (1991) Relationship of anemia to Balkan endemic nephropathy. Kidney Int. -Supplement. 34: S44-45.
Hsu, D.Z.; Wana, C. H.; Hsu, H. F.; Lin, Y. M; Liu, M. Y. (2008). The prophylactic protective effect of sesamol against ferric–nitrilotriacetate-induced acute renal injury in mice. Food Chem. Toxicol. 46, 2736–2741.
Hung, T. H., Chang, Y. M., Sung, H. Y. and Chang, C. T. (2002) Purification and characterization of hydrolase with chitinase and chitosanase activity from commercial stem bromelain. J. Agric. Food Chem. 50: 4666-4673.
Il’ina, A. V. and Varlamov, V. P. (2004) Hydrolysis of chitosan in lactic acid, Appl Biochem. Microbiol. 40: 300-303.
Irhuma, A., Gallagher, J., Hackett, T. J. and Mchale, A. P. (1991) Studies on β-N-acetylglucosaminidase activity produced by Streptomyces hygroscpicus. Biochim. Biophys. Acta. 1074: 1-5.
Izume, M., Nagae, S., Kawagishi, H., Mitsutomi, M., Ohtakara, A. (1992) Action Pattern of Bacillus sp. No. 7-M chitosanase on partially N-acetylated chitosan. Biosci. Biotech. Biochem. 56: 448-453.
Jackson, L., Kofman, S., Wesis, A. and Brodovsky, H. (1964) Aristolochic acid (NSC-50413): Phase I clinical study. Cancer Chemotherapy Representation. 42: 35-37.
Jeuniaux, C. (1966) Chitinase. In Methods In Enzymology (Neufeld, G.F. and Ginsburg, V. Eds).. Academic Press, New York. Vol. 8, p.644-654.
Jin, Y. L., Jo, Y. Y., Kim, K. Y., Shim, J. H., Kim, Y. W. and Park, R. D. (2002) Purification and characterization of beta-N-acetylhexosaminidase from rice seeds. J Biochem. Mol. Biol. 35(3): 313-319.
Jing, S. B., Li, L., Ji, D., Takiguchi, Y. and Yamaguchi, T. (1997) Effect of chitosan on renal function in patients with chronic renal failure. J. Pharm. Pharmacol. 49(7): 721-723.
Jones, C. S. and Kosman, D. J. (1980) Purification, properties, kinetics, and mechanism of β-N-acetylglucosaminidase from Aspergillusniger. J. Biol. Chem. 255: 11861-11869.
Kabanda, A., Jadoul, M., Lauwerys, R., Bernard, A. and van Ypersele de Strihou, C. (1995) Low molecular weight proteinuria in Chinese herbs nephropathy. Kidney Int. 48: 1571-1576.
Kabayashi, M., Watanabe, T., Suzuki, S. and Suzuki, M. (1990) Effect of N-acetyl-chitohexaose against Candida albicans infection of tumor-bearing mice. Microbiol. Immunol. 34: 413-426.
Kashif, W., Siddiqi, N., Dincer, A. P., Dincer, H. E. and Hirsch, S. (2003) Proteinuria: How to evaluate an important finding. Cleve. Clin. J. Med. 70: 535-47.
Kauss, H., Jeblick, W. and Domard, A. (1989) The degrees of polymerization and N-acetylation of chitosan determine its ability to elicit callose formation in suspension cells and protoplasts of Catharanthus roseus. Planta. 178: 385-392.
Kendra, D. F. and Hadwiger, C. A. (1984) Characterization of the smallest chitosan oligomer that is maximally antifugal to Fusarium solani and elicits pisatin formation in Pisum sativum. Exp. Mycol. 8: 276-284.
Kim, J. S., Kim, Y. Q. Ryu, H. T., Kwak, Y. S., Lee, J. Y. and Kang, H. (2003) Isolation of stress-related genes of rubber particles and latex in fig tree (Ficus carica) and their expressions by abiotic stress of plant hormone treatments. Plant Cell Physiol. 44: 412-414.
Kim, S. K. and Rajapakse, N. (2005). Enzymatic production and biological activities of chitosan oligosaccharides (COS): A review. Carbohydr. Polym. 62(4):357-368.
Kimura, S. (1976) Insect haemolymph exo-β- N- acetylglucosaminidase Bombyx mori. Biochim. Biophys. Acta. 446: 399-406.
Kitchen, B. J. and Masters, C. J. (1985) Purification and properties of bovine marmmary glandβ-N-acetylglucosaminidase. Biochem. Biophys. Acta. 831: 125-132.
Kliesch, U., Danford, N. and Adler, I. D. (1981) Micronucleus test and bone-marrow chromosome analysis: a comparison of 2 methods in vivo for evaluating chemically induced chromosomal alterations. Mutat Res. 80(2):321-32.
Kobayashi, M., Watanabe, T., Suzuki, S., Suzuki, M. (1990) Effect of N-acetylchitohexaose against Candida albicans infection of tumor-bearing mice. Microbiol. Immumol. 34: 413-426.
Koga, D. (1998) Chitin enzymology-chitinase. In Advances in Chitin Science (Chen, R.H., Chen, H.C. Eds), Scientific Advisory Program Committee. Taipei, 3: 16-23.
Koga, D., Nakashima, M., Matsukura, T., Kimura, S. and Ide, A. (1986) Purification and properties of β-N-acetylglucosaminidase from alimentary canal of the silkworm, Bombyx mori. Agric. Biol. Chem. 50: 2357-2368.
Koguchi, T., Koguchi, H., Nakajima, H., Takano, S., Yamamoto, Y., Innami, S., Maekawa, A. and Tadokoro, T. (2004) Dietary fiber suppresses elevation of uric acid and urea nitrogen concentrations in serum of rats with renal dysfunction induced by dietary adenine. Int. J. Vitam. Nutr. Res. 74(4): 253-263.
Krumbiegel, G., Hallensleben, J., Mennicke, W. H., Rittmann, N. and Roth, H. J. (1987) Studies on the metabolism of aristolochic acids I and II. Xenobiotica. 17: 981-991.
Kuroiwa, T., Ichikawa, S., Sato, S., Hiruta, O., Sato, S. and Mukataka, S. (2002) Factors affecting the composition of oligosaccharides produced in chitosan hydrolysis using immobilized chitosanases, Biotechnol. Prog. 18: 969-974.
Laemmli, U. K. (1970) Cleavage of structural proteins during the assesmbly of the head of bacteriophage T4. Nature. 227: 680-685.
Lai, L. S., Wang, D. J., Chang, C. T. and Wang, C. H. (2006) Catalytic characteristics of peroxidase from wheat grass. J. Aagric. Food Chem. 54:8611-8616.
Le Hir, M., Dubach, U. C. and Schmidt, U. (1979) Quantitative distribution of lysosomal hydrolases in the rat nephron. Histochemistry. 63:245-251.
Leaback, D. H. and Walker, P. G. (1961) Studies on glucosaminidase. 4. The fluorometric assay of N-acetyl-beta-glucosaminidase. Biochem. J. 78: 151-156.
Lebeau, C., Arlt, V. M., Schmeiser, H. H., Boom, A., Verroust, P. J., Devuyst, O. and Beauwens, R. (2001) Aristolochic acid impedes endocytosis and induces DNA adducts in proximal tubule cells. Kidney Int. 60: 1332-1342.
Lebeau, C., Debelle, F. D., Arlt, V. M., Pozdzik, A., De Prez, E. G., Phillips, D. H., Deschodt-Lanckman, M. M., Vanherweghem, J. L. and Nortier, J. L. (2005) Early proximal tubule injury in experimental aristolochic acid nephropathy: functional and histological studies. Nephnol. Dial. Transplant. 20: 2321-2332.
Lee, T. Y., Wu, M. L., Deng, J. F. and Hwang, D. F. (2002) High-performance liquid chromatographic determination for aristolochic acid in medicinal plants and slimming products. J. Chromatogr. B. Biomed. Sci. Appl. 766: 169-174.
Lehoux, J. G. and Grondin, F. (1993) Some effects of chitosan on liver function in the rat. Endocrinology, 132 (3): 1078-1084.
Leung, D. W. M. (1992) Involvement of chitinase sexual reproduction of higher plant. Phytochemistry 31: 1899-1900.
Levry, G. A. and McAllan, A. (1962) Some plant glycosidase. Nature. 195: 387.
Li, S. C. and Li, Y. T. (1970) Studies on the glycosidase of jack bean meal: Ⅲ. Crystallization and properties of β-N-acetylgucosaminidase. J. Biol. Chem. 245: 5153-5160.
Linko-Lopponen, S. (1986) Fluorometric measurement of urinary N-acetyl-beta-D-glucosaminidase and its correlation to uremia. Clin. Chim. Acta, 160 (2): 123-127.
Linthorst, H. J. M. (1991) Pathogenesis-related proteins of plants. Crit. Rev. Plant Sci. 10: 123-150.
Liu, Y. D. and Speer, R. J. (1977) Chemical modification of L-asparaginase, Implication of tyrosyl and histidyl residues in the active site of E. coli asparaginase. J. Chinese Biochem. Soc. 6: 61-64.
Loeb, W. F., Das, S. R., Harbour, L. S., Turturro, A., Bucci, T. J. and Clifford, C. B. (1996) Clinical biochemistry in Mohr U., Fungworth D. L., Dungworth D. L., Capen C. C. (eds.) Pathobiology of the aging rat. Washington, pp.7-24.
Lu, J. X., Prudhommeaux, F., Meunier, A., Sedel, L. and Guillemin, G. (1999) Effects of chitosan on rat knee cartilages. Biomaterials. 20: 1937-1944.
MacGregor, J. T., Wehr, C. M., and Gould, D. H. (1980). Clastogen induced micronuclei in peripheral blood erythrocytes: The basis of an improved micronucleus test. Environ. Mutag. 2(4) :509-514.
Marsilio, R., Dall'Amico, R., Giordano, D., Murer, L., Montini, G., Ros M., Dussini, N., Zacchello, G., Bacelle, L. and Plebani, M. (1999) Rapid fetermination of creatinine in serum and urine by ion pair high-performance liquid chromatography. Int. J. Clin. Lab. Res. 29(3):103-109.
Martin, M. N. (1991) The latex of Hevea brasiliensis contains high levels of both chitinases and chitinase/lysozymes. Plant Physiol. 95: 469-476.
Masson, J. Y., Boucher, I., Neugebauar, W. A., Ramotar, D. and Brzezinski, R. (1995) A new chitosanase gene from a Nocardioides sp. is a third membrane of glycosyl hydrolase family 46. Microbiology. 141: 2629-2635.
McFarkane, E. F., Mcfarlane, D. R. and Kennedy, I. R. (1984) Isolation of -N-acetyl-D-hexosaminidase from lupin seed. Phytochemisty. 23: 2431-2433.
Mckenzie, H. A. and Dawson, R. M. C. (1969) pH, buffer and physiological media. In data for Biological Research (Dawson, R.M.C., Elliott, D.C., Elliott, W. H. and Jones, K.M. ods.) Clarendon Press, Oxford. pp.476-508.
Mengs, U. (1983) On the histopathogenesis of rat fore stomach carcinoma caused by aristolochic acid. Arch. Toxicol. 52:209-220.
Mengs, U. (1987) Acute toxicity of aristolochic acid in rodents. Arch. Toxicol. 59(5): 328-331.
Mengs, U. and Stotzem, C. D. (1992) Toxicity of aristolochic acid - a subacute study in male rats. Med. Sci. Res. 20: 223-224.
Mengs, U. and Stotzem, C. D. (1993) Renal toxicity of aristolochic acid in rats as an example of nephrotoxicity testing in routine toxicology. Arch. Toxicol. 67: 307-311.
Michael, F. C. and Jonathan, L. T. (2000) Proteinuria in adults: A diagnostic Approach. Am. Fam. Physician. 62:1333-1342.
Mihara, S. (1961) Change in glucosamine content of chlorella cells during there life cycle. Plant Cell Physiol. 2: 25-29.
Miles, E. W. (1977) Modification of histidyl residues in proteins by diethyl pyrocarbonate. In Methods in Enzymology (Hirs, C.H.W., Timasheff, S.N. Eds) Academic press, New York, Vol. 47, pp. 431-454.
Miller, A. L., Kress, B. C., Stein, R., Kinnon, C., Kern, H., Schneider, J. A. and Harms, E. (1981) Properties of N-acetyl-β-D-hxosaminidase from isolated normal and I-cell lysosomes. J. Biol. Chem. 256: 9352-9362.
Mommsen, T. P. (1980) Chitinase and β-N-acetylglucosaminidase from the digestive fluid of spider,Cupiennius salei. Biochem. Biophys. Acta. 612: 361-372.
Monaghan, R. L., Eveleigh, D. E., Tewari, R. F. and Reese, E. T. (1973) Chitosanase, a novel enzyme. Nature New Biol. 245: 78-80.
Moreno, J. J. (1993) Effect of aristolochic acid on arachidonic acid cascade and in vivo models of inflammation. Immunopharmacology. 26:1-9.
Morgan, D. B., Dillon, S. and Payne, R. B. (1978) The assessment of glomerular function: creatinine clearance or plasma creatinine? Postgraduate Med. J. 54: 302-310.
Morgera, S., Haase, M., Rocktaschel, J., Bohler, T., von Heymann, C., Vargas-Hein, O., Krausch, D., Zuckermann-Becker, H., Muller, J. M., Kox, W. J. and Neumayer, H. H. (2003) High permeability haemofiltration improves peripheral blood mononuclear cell proliferation in septic patients with acute renal failure. Nephnol. Dial. Transplant. 18: 2570-2576.
Muzzarelli, R. A. A. (1977) Chitin. Pergamon Press, Oxford, p. 87
Muzzarelli, R. A. A. (1985) Determination of the degree of acetylation of chitosan by first derivative ultraviolet spectrometry. Carbohydr. Polym. 5: 461-469.
Muzzarelli, R. A. A. (1996) chitosan-based dietary foods. Carbohydr. Polym. 29: 309-316.
Muzzarelli, R. A. A., Barontin, G. and Roccheti, R. (1978) Isolation of lysozme on chitosan. Biotech. Bioeng. 20: 89-94.
Muzzarelli, R. A. A., Tomasetti, M. and Ilari, P. (1994) Depolymerization of chitosans with the aid of papain. Enzyme Microb. Technol. 16 : 110-114.
Muzzarelli, R. A. A., Tomasetti, M. and Ilari, P. (1995) Depolymerization of chitosan and substituted chitosans with the aid of a wheat germ lipase preparation. Enzyme Microb. Technol. 17: 541-545.
Nanjo, F., Ishikawa, M., Katsumi, R. and Sakai, K. (1990) Purification, Properties and transglycosylation reaction of b-N-acetylhexosaminidase from Nocardia orientalis. Agric. Biol. Chem. 54: 899-906.
Neuberger, A. and Rivers, R. V. (1939) The hydrolysis of glucosaminidase by an enzyme in Helix pomatia. Biochem. J. 33: 1580-1586.
Nishimura, T., Eto, E. and Yamada, T. (1986) European patent application. 863, 096, 095.
Nortier, J. L., Deschodt-Lanckman, M. M., Simon, S., Thielemans, N. O., de Prez, E. G., Depierreux, M. F., Tielemans, C. L., Richard, C., Lauwerys, R. R., Bernard, A. M. and Vanherweghem, J. L. (1997) Proximal tubular injury in Chinese herbs nephropathy: monitoring by neutral endopeptidase enzymuria. Kidney Intl. 51: 288-293.
Nortier, J. L., Martinez, M. C., Schmeiser, H. H., Arlt, V. M., Bieler, C. A., Petein, M., Depierreux, M. F., De Pauw, L., Abramowicz, D., Vereerstraeten, P., Vanherweghem, J. L. (2000) Urothelial carcinoma associated with the use of a Chinese herb (Aristolochia fangchi). New. Engl. J. Med. 342(23): 1686-1692.
Ohtakara, A., Izume, M. and Mitsutomi, M. (1988) Action of microbial chitinases on chitosan with different degrees of deacetylation. Agric. Biol. Chem. 52: 3181-3182.
Oikawa, A., Itoh, E., Ishihara, A. and Iwamura, H. (2003) Purification and characterization of beta-N-acetylhexosaminidase from maize seedlings. J. Plant Physiol. 160: 991-9.
Okada, S. and O’Brien, J. S. (1969) Tay-Sachs disease: Generalized absornce of β-N-acetylhexosaminidase component. Sceince. 165: 698-700.
Ordentlich, A., Elad, Y. and Chet, I. (1988) The role of chitinase of Serratia marcescens in biocontrol of Sclerotium rolfsii. Phytopathology. 78: 84-87.
Orlacchio, A., Maffel, C., Emiliani, C. and Reinosa, J. A. (1985) On the active site of b-hexosaminidase from latex of Ficus glavrata. Phytochemistry. 24: 659-662.
Osswald, W. F., Shapiro, J. P., Doostdar, H., McDonald, R. E., Niedz, R. P., Nairn, C. J. C., Hearn, J. and Mayer, R. T. (1994) Identification and characterization of acidic hydrolases with chitinase and chitosanase activities from sweet orange callus tissue. Plant Cell Physiol. 35(5): 811-820.
Osswald, W. F., Shapiro, J. P., Mcdonald, K. E., Niedz, R. P. and Mayer, R. T. (1993) Some citrus chitinases also possess chitosanase activities. Experientia. 49: 889-892.
Ouakfaoui, S. E. and Asselin, A. (1992a) Diversity of chitosanase activity in cucumber. Plant Sci. 85: 33-41.
Ouakfaoui, S. E. and Asselin, A. (1992b) Multiple forms of chitosanase activities. Phytochemistry. 31: 1513-1518.
Papineau, A. M., Hoover, D. G., Knorr, D. and Farkas, D. F. (1991) Antimicrobial effect of water-soluble chitosans with high hydrostatic pressure. Food Biotechnol. 5: 45-57.
Park, P. J., Je, J. Y. and Kim, S. K. (2003) Angiotension 1 converting enzyme (ACE) inhibitory activity of heaven-chitooligosaccharides prepared from partially different deacetylated chitosans. J. Agric. Food Chem. 51: 4920-4934.
Pegg, G. F. and Young, D. M. (1982) Purification and characterization of chitinase enzymes from healthy and Verticillium albo-atrum infeeted tomato plants and from V. albo-atrum. Physiol. Plant Pathol. 21: 289-309.
Pelletier, A. and Sygusch, J. (1990) Purification and characterization of three chitosanase activities from Bacillus megaterium P1. Appl. Environ. Microbiol., 56: 844-848.
Pelletier, A., Lemire, I., Sygusch, J., Chornet, E. and Overend, R. P. (1990) Chitin/chitosan transformation by theromo-mechano-chemical treatment including characterization by enzymatic depolymerisation. Biotechnol. Bioeng. 36: 310-315.
Peters, G. and Hedwall, P. R. (1963) Aristolochic acid intoxication : A new type of pairment of urinary concentration ability. Arch. Int. Pharmacol. 145: 334-335.
Pocsi, I., Kiss, L. and Nanasi, P. (1990) Studies on the N-acetyl-β-D-hexosaminidase B from germinating Lupinus luteus L. seed: Ⅰ. Purification and characterization. Biochem. Biophys. Acta. 1039:110-118.
Pocsi, I., Kiss, L. and Nanasi, P. (1990) Studies on the N-acetyl-β-Dhexosaminidase B from germinating Lupinus luteus L. seed: Ⅱ. Mechanism and inhibition with some 2-acetamido-2-deoxyalono (1 4) lactones. Biochem. Biophys. Acta. 1039: 119-122.
Price, J. S. and Storck, R. (1975) Production, purification and characterization of an extracellular chitosanase from streptomyces. J. Bacteriol. 124: 1574-1585.
Priem, B. and Gross, K. C. (1992) Mannosyl and xylosyl-containing glycans promote tomato (Lycopersicon esculentum Mill) fruit ripening. Plant Physiol. 98: 399-401.
Qi, U. F., Xu, Z. R., Li, Y. Jiang, X. and Han, X. Y. (2005) In vitro effects of chitosan nanoparticles on proliferation of human gastric carcinoma cell line MGC803 cells. World J. Gastroenterol. 11(33): 5136-5141.
Quin, C., Du, Y., Xiao, L., Li, Z. and Gao, X. (2002) Enzymic preparation of water-soluble chitosan and their antitumor activity. Itl. J. Biol. Marcromol. 31: 111-117.
Raicevic, S., Trnacevic, S., Hranisavljevic, J. and Vucelic, D. (1991) Renal function, protein excretion, and pathology of Balkan endemic nephropathy. II. Protein excretion. Kidney Int. – Supplement. 34: S52-56.
Reginster, F., Jadoul, M. and van Ypersele de Strihou, C. (1997) Chinese herbs nephropathy presentation, natural history and fate after transplantation. Nephnol. Dial. Transplant. 12: 81-86.
Ricci, Z., Ronco, C., D'Amico, G., De Felice, R., Rossi, S., Bolgan, I., Bonello, M., Zamperetti, N., Petras, D., Salvatori, G. Dan, M. and Piccinni, P. (2006) Practice patterns in the management of acute renal failure in the critically ill patient: an international survey. Nephnol. Dial. Transplant. 21: 690-696.
Ride, J. P. and Drysdale, R. B. (1972) A rapid method for the chemical estimation of filamentous fungi in plant tissue. Physiol. Plant Pathol. 2: 1-15.
Robbins, B. H. and Lamson, P. D. (1934) Further studies on the proteolytic enzyme content of latex from the fig and related trees. J. Biol. Chem. 102(2): 725-728.
Ronald, L. and Koretz, M. D. (1992) Chronic hepatitis: science and superstition. In: Current Hepatology (ed. by Gitnick G.), Mosby-Year, Chicago, 12: 53-74.
Rozeboom, H. J., Budiani, A., Beintema, J. J. and Dijkstra, B. W. (1990) Crystallization of hevamin, and enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex. J. Mol. Biol. 212: 441-443.
Rucker, V. G. and Chung, B. S (1975) [Aristolochic acids from Aristolochia manshuriensis (author's transl)]. Planta Medica. 27: 68-71.
Saito, J. I., kita, A., Higuchi, Y., Nagata, Y., Ando, A. and Miki, K. (1999) Crystal structure of chitosanase from Baccillus cirulans MH-K1 at 1.6-Á resolation and its salt with acid: conformation characterization of polymorph and helical structures as viewed from the conformation-dependent 13C chemical shifes. Macrol. 20: 2424-2430.
Sashiwa, H., Saimoto, H., Shigemasa, Y., Ogawa, R. and ToKura, S. (1990) Lysozyme susceptibility of partially deacetylated chitin. Int. J. Biol. Marcromol. 12: 295-296.
Sato, N., Takahashi, D., Chen, S-M, Tsuchiya, R, Mukoyama, T, Yamagata, S-i, Ogawa, M., Yoshida, M., Kondo, S., Satoh, N. and Ueda, S. (2004) Acute nephrotoxicity of aristolochic acids in mice. J. Phar. Pharmacol. 56: 221-229.
Schmeiser, H. H., Bieler, C. A., Wiessler, M., van Ypersele de Strihou, C. and Cosyns, J. P. (1996) Detection of DNA adducts formed by aristolochic acid in renal tissue from patients with Chinese herbs nephropathy. Cancer Res. 56: 2025-2028.
Schneider, R., Raff, U., Vornberger, N., Schmidt, M., Freund, R., Reber, M., Schramm, L., Gambaryan, S., Wanner, C., Schmidt, H. H. and Galle J. (2003) L-Arginine counteracts nitric oxide deficiency and improves the recovery phase of ischemic acute renal failure in rats. Kidney Int. 64: 216-225.
Scigelova, M. and Crout, D. H. G. (1999) Microbial β-N-acetylhexosaminidases and their biotechnological applications, Enzyme Microb. Technol. 25. 3–14.
Seino, H., Tsukud, K. and Shimasue, Y. (1991) Properties and action pattern of a chitosanase from Bacillus sp. 7I-7S. Agric. Biol. Chem. 55:2421-2423.
Seo, W. G., Pae, H. O., Kim, N. Y., Oh, G. S., Park, I. S., Kim, Y. H., Kim, Y. M., Lee, Y. H., Jun, C. D. and Chung, H. T. (2000) Synergistic cooperation between water-soluble chitosan oligomers and interferon-r for induction of nitric oxide synthesis and tumoricidal activity in murine peritoneal macropages. Cancer Lett. 159: 189-195.
Shahid, F., Vidana Aracchchi, J. K. and Jeon, Y. J. (1999) Food applications of chitin and chitosan. Trends Food Sci. Technol. 10: 37-51.
Shaw, J. F. and Chang, C. M. (1988) The effect of chemical modification and additives on the stabilities of lipase from Aspergillus niger. Bot. Bull. Acad. Sin. 29: 101-107.
Shingfield, K. J. and Offer, N. W. (1999) Simultaneous determination of purine metabolitesm, creatinine and pseudouridine in ruminant urine by reversed-phase high-performance liquid chromatography. J Chromatogr. B. Biomed. Sci. Appl. 723 (1-2): 81-94.
Shirui, M., Xintao, S., Florian, U., Michael, S., Dianzhou, B. and Thomas, K. (2004) The depolymerization of chitosan: Effects on physicochemical and biological properties, Int. J. Pharm. 281: 45-54.
Simerville, J. A., Maxted, W.C. and Phira, J. J. (2005) Urinalysis. Am Fam Physician. 71: 1153-61.
Singh, A., Kirubakaran, I. and Sakthivel, N. (2007) Heterologous expression of new antifungal chitinase from wheat. Protein Expr. Purif. 56: 100-109.
Skrha, J., Haas, T., Sperl, M., Stibor, V. and Stolba, P. (1991) A six-year follow-up of the relationship between N-acetyl-beta-glucosaminidase and albuminuria in relation to retinopathy. Diabetic Medicine. 8:817-821.
Sluyteerman, L. A., Wijdenes, J. (1970) An agarose mercurial column for the separation of mercapto papain and nonmercapto papain. Biochim, Biophysm Acta. 200: 593-595.
Smith, P., Krohn, R. I., Hermanson, G. R., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J. and Klenk, D. C. (1985) Measurement of protein using bicinchonic acid. Anal. Biochem. 15: 76-85.
Somashekar, D. and Joseph, R. (1996) Chitosanase-properties and application: a review. Biosci. Technol. 55: 35-45.
Somashekar, D. and Joseph, R. (1997) A new spectrophotometric method for assay for chitosanase based on Calcofluor White dye binfing. Carbohydr. Polym. 43: 343-346.
Spande, T. F. and Witkop, B. (1976) Determination of the tryptophan content of proteins with N-bromosuccimide：In Methods in Enzymology (Hirs, C. H. W. Ed) Academic Press, Vol. 11, pp. 489-494.
Stanley, W. L., Watters, G. G., Chan, B. G. and Mercer, J. M. (1975) Lactase and other enzymes bound to chitin with glutaldehyde. Biotech. Bioeng. 17: 315-326.
Stolarek, I., Howey, J. E. and Fraser, C. G. (1989) Biological variation of urinary N-acetyl-beta-D-glucosaminidase: practical and clinical implications. Clin. Chem. 35: 560-563.
Su, J. C. (1965) Carbohydrate metabolism in the shoots of bamboo, Lelba oldhami. IV. A structural study of cell wall polysaccharides. Bot. Bull. Acad. Sinica 6: 153-159.
Su, J. C. Wu, J. L. and Yang, C. L. (1977) Purification and characterization of sucrose synthase from the shoot of bamboo Leleba oldhami. Plant Physiol. 60: 17-21.
Su, J. C., Yang, C. L., Sung, H. Y., Chang, C. T. and Yeh, D. B. (1973) Biochemical mechanism of plant cell wall maturation. Proc. Natl. Sci. Counc. 6: 1-12.
Su, J. C., Yuan, H. F., Sung, H. Y. (1968) Carbohydrate metabolism in the shoots of bamboo, Leleba oldhami. V. The callose synthesizing system. J. Chinese Agric. Chem. Soc. Sp. Iss. 1-11.
Subroto, J., Van Koningsveld, G. A., Scheuder, H. A., Soedjanaatmadja, U. M. and Beintema, J. J. (1996) Chitinase and ß-1,3-glucanase in the lutoid-body fraction of Hevea latex. Phytochemistry. 43: 29-37.
Sugano, M., Yoshida, K., Hashimoto, M., Enomoto, K. and Hirano, S. (1992) Hypocholesterolemic activity of partially hydrolyzed chitosan in rats. In: (C.J. Brine, P.A. Sandford and J.P. Zikakis, Editors), Advances in Chitin and Chitosan, Elsevier, London, pp. 472-478.
Suzuki, K., Okawa, Y., Hashimoto, K., Suzuki, S. and Suzuki, M. (1984) Protecting effect of chitin and chitosan on experimentally induced murine candidiasis. Microb. Immunol. 28: 903-912.
Suzuki, K., Tokoro, A., Okawa, Y., Suzuki, S. and Suzuki, M. (1986) Effect of N-acetylchito-oligosaccharides on activation of phagocytes. Microb. Immunol. 30: 777-787.
Suzuki, K., Tokoro, A., Okawa, Y., Suzuki, S., and Suzuki, M. (1986c) Effect of N-acetyl-chito-oligosaccharides on activation of phagocytes. Microliol. Immunol. 30: 777-787.
Suzuki, K., Toloro, A., Okawa, Y., Suziki, S. and Suziki, M. (1985) Enhancing effects of N-acetyl-chito-oligosaccharides on the active oxygen-generating and microbicidal activities of peritoneal exudates cells in mice. Chem. Pharm, Bull. 33: 886-889.
Suzuki, K., Toloro, A., Okawa, Y., Suziki, S. and Suziki, M. (1986a) Effect of N-acetyl-chito-oligosaccharides on activation of phagocytes. Microbiol. Immunol. 30 (8): 777-787.
Suzuki, S., Okawa, Y., Tokoro, A., Suzuki, K. and Suzuki, M. (1986b) Immunogotentiating effects of N-acetyl chito-oligosaccharides. In Chitin in Nature and Technology (Muzzarelli, R. A. A., Jeuniaux, C. and Gooday, G. Eds) pp.485-492, Plenum Press, New York.
Tassi, C., Mancuso, F., Feligioni, L., Marangi, M. and Capodicasa, E. (2004) Expression modes of urinary N-acetyl-beta-D-glucosaminidase in patients with chronic renal insufficiency. Clin. Chim. Acta. 346: 129-133.
Tates, A. D., Dietrich, A. J. J., and De Vogel, N. (1983). A micronucleus method for detection of meiotic micronuclei in male germ cells of mammals. Mutat Res. 121(2) : 131-138.
Terbojevich, M., Cosani, A. and Muzzarelli, R. A. A. (1996) Molecular parameters of chitosanase depolymerized with the aid of papain. Carbohydr. Polym. 29: 63-68.
The U.S. Food and Drug Administration’s (2000). Mammalian Erythrocyte Micronucleus Test. “Toxicological Principles for the Safety Assessment of Food Ingredients Redbook , 2000 “.
Tokoro, A., Kobayashi, M., Tatewaki, N., Suzuki, K., Okawa, Y., Milami, T., Suzuki, S. and Suzuki, M. (1989) Protective effect of N-acetyl-chitohexaose on Listeria monocyrogenes infection in mice. Microbiol. Immunol. 33: 357-367.
Tokoro, A., Tatewaki, N., Suzuki, K., Mikami, T., Suzuki, S. and Suzuki, M. (1988) Groth-inhibitory effect of hexa-N-acetylchitohexaose and chitohexaose against Meth-A solid tumor. Chem. Pharm. Bull. 36: 784-790.
Tominaga, Y. and Tsujisaka, Y. (1975) Purification and some enzymatic properties of the chitosanase from Baciius R-4 which lyses Rhizopus cell walls. Biochem. Biophys. Acta. 410: 145-155.
Trudel, J. and Asselin, A. (1989) Detection of chitinase activity after polyacrylamide gel electrophoresis. Anal. Biochem. 178: 362-366.
Tsai, G. J. and Su, W. H. (1999) Antibacterial activity of shrimp chitosan against Escherichia coli. J. Food Prot. 62: 239-243.
Tsai, G. J., Wu, Z. Y. and Su, W. H. (2000) Antibacterial activity of a chitooligosaccharide mixture prepared by cellulase digestion of shrimp chitosan and its application to milk preservation. J. Food Prot. 63:747-752.
Tsuji, A., Kinoshita, T. and Hoshino, M. (1972) Analytical chemical studies on aminosugars. I. Determination of hexosamines using 3-methyl-2-benzothiazolone hydrochloride. Chem. Pharm. Bull. 2:7-15.
Udea, M. and Arai, M. (1992) Purification and some properties of chitinase from Aeromonase sp. 10S-24. Biosci. Biotech. Biochem.56: 460-464.
Ueno, R. and Yuan, C. S. (1991) Purification and properties of neutral β-Nacetyl-glucosaminidase from carp blood. Biochem. Biophys. Acta. 1074: 79-84.
Van Parijs, J., Broekaert, W. F., Goldstein, I. J. and Peumans, W. J. (1991) Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex. Planta. 183: 258-264.
van Ypersele de Strihou, C. (1998) Chinese herbs nephropathy or the evils of nature.[see comment]. Am. J. Kidney Dis. 32: 1-11.
Vandrysperre, W., Hilderson, H. K., Callens, M. and Debruyne, C. K. (1989) Woodward’s reagent with D-xylose isomerase: modification of an active site carboxylase residue. Biochem. J. 260: 163-169.
Vanhaelen, M., Vanhaelen-Fastre, R., But, P. and Vanherweghem, J. L. (1994) Identification of aristolochic acid in Chinese herbs. Lancet. 343:174.
Vanherweghem, J. L., Abramowicz, D., Tielemans, C. and Depierreux, M. (1996) Effects of steroids on the progression of renal failure in chronic interstitial renal fibrosis: a pilot study in Chinese herbs nephropathy. Am. J. Kidney Dis. 27(2): 209-215.
Vanherweghem, J. L., Depierreux, M., Tielemans, C., Abramowicz, D., Dratwa, M., Jadoul, M., Richard, C., Vandervelde, D., Verbeelen, D. and Vanhaelen-Fastre, R. (1993) Rapidly progressive interstitial renal fibrosis in young women: association with slimming regimen including Chinese herbs. [see comment]. Lancet. 341: 387-391.
Vanherweghem, J. L., Tielemans, C., Simon, J. and Depierreux, M. (1995) Chinese herbs nephropathy and renal pelvic carcinoma. Nephnol. Dial. Transplant. 10: 270-273.
Venkat, K. K. (2004) Proteinuria and microalbuminuria in adult: Significance, evaluation and treatment. South. Med. J. 97: 969-79.
Verpoorate, J. A. (1974) Isolation and characterization of the major N-β-acetyl- glucosaminidase from human plasma. Biochemistry. 13:793-799.
Viswanatha, T. and Lawson, W. B. (1961) The reaction of N-bromosuccimimide on chymotrypsin. Arch. Biochem. Biophys. 93: 128-134.
Welches, W. R. and Baldwin, T. D. (1981) Active center studies on bacterial luciferase：modification of the enzyme with 2,4-dinitroflurobenzene. Biochemistry, 20: 512-515.
Westhuyzen, J., Endre, Z. H., Reece, G., Reith, D. M., Saltissi, D. and Morgan, T. J. (2003) Measurement of tubular enzymuria facilitates early detection of acute renal impairment in the intensive care unit. Nephnol. Dial. Transplant. 18: 543-551.
Whitaker, J. R. (1959) Properties of the milk-clotting activity of ficin. Food Technol. 13: 86-92.
William, C. (1958) Characterization of ficin. Nature. 182: 659-660.
Woollen, J. W. and Turner, P. (1965) Plasma N-acetyl-beta-glucosaminidase and beta-glucuronidase in health and disease. Clin. Chim. Acata. 12: 671-683.
Yalpani, M. and Pantaleone, O. (1994) An examination of the unusual susceptibilities of aminoglycans to enzymatic hydrolysis. Carbohydr. Res. 256: 159-175.
Yamasaki, Y., Hayashi, I., ohta, Y., Nakagawa, T., kawamakai, M. and Matsuda, H. (1993) Purification and mode of action of chitosanolytic enzyme from enterobacter sp. G-1. Biosci. Biotech. Biochem. 57: 444-449.
Yang, C. S., Lin, C. H., Chang, S. H. and Hsu, H. C. (2000) Rapidly progressive fibrosing interstitial nephritis associated with Chinese herbal drugs. Am. J. Kidney Dis. 35(2): 313-318.
Yi, C. K. (1981) Increase in β-N-acetylglucosaminidase activity during germination of cotton seeds. Plant Physiol. 67: 68-73.
Yoon, H. J., Moon, M. E., Park, H. S., Kim, H. W., Im, S. Y., Lee, J. H. and Kim, Y. H. (2008) Effects of chitosan oligosaccharide (COS) on the glycerol-induced acute renal failure in vitro and in vivo. Food Chem. Toxicol. 46: 710-716.
Yoshihara, K., Hosokawa, J., Kubo, T., Nishiyama, M. and Koba, Y. (1992) Purification and properties of a chitosanase from Pseudomonas sp. H-14 Biosci. Biotech. Biochem. 56: 972-973.
Zeiler M., Bock A., Zurcher R., Gratwohl A. and Thiel G. (1994) Plasma creatinine for the evaluation of recovery of glomerular filtration rate after discontinuation of cyclosporine A in bone marrow transplantation: results of a prospective study. Transplant. Pro. 26: 2590-2593.
Ziai, S. A., Mooraki, A. and Mahmoudian, M. (2002) Gentamicin reduces serum ACE activity in patients with normal kidney function. Am. J. Nephnol. 22: 487-490.