植物中廣泛存在的親醣蛋白lectins過去被認為是影響養份吸收的“抗營養物質(anti-nutrient)”，然而近年來的研究卻認為這些可與細胞表面特定醣類結構結合的蛋白質，能夠引起對腫瘤細胞的毒殺作用或抑制其生長，顯示其可能作為對抗惡性腫瘤工具的潛力。本研究利用Lectin可以專一辨識不同醣類結構的特性，建立以聚丙烯醯胺結合不同單醣(包含D-mannose、N-acetyl-D-glucosamine、N-acetyl-D-galactosamine及L-fucose)之共價聚合物作為篩選Lectin之專一性配體(ligand)，利用酵素聯結吸附分析法(enzyme-linked adsorbent assay)對植物材料進行篩選，並分別以Con A、WGA、SBA及UEA I等已知Lectin作為正對照組。相較於傳統的血球凝集測試方法，本研究所建立的醣聚合物聯結分析可篩選與辨別樣品中是否具有對特定醣基結構專一性結合能力，且可避免血球來源與表面結合部位無法掌握的缺點。利用此篩選方法自29種植物材料中篩選出數種對特定醣基結構具有專一性結合能力之標的植物材料。其中，木瓜籽中具有對N-acetyl-D-galactosamine (GalNAc)專一性結合活性之Lectin，藉由硫酸銨沉澱劃分、DEAE離子交換管柱層析及重複利用膠體過濾管柱層析等步驟進行純化分離，並將它命名為CPL (C. papaya lectin)。以不同醣類抑制血球凝集反應的結果顯示，CPL對GalNAc與Lactose具有專一性結合能力。進一步利用表面電漿共振技術分析木瓜籽親醣蛋白對GalNAc之親和動力學參數，其平衡解離常數KD達5.5 × 10^-9 M，顯示CPL對GalNAc具有極高的親和力。利用分子篩高效液相層析(Size-exclusion HPLC)分析CPL之分子量得知其原態約為804 kDa，並由38-及40- kDa之次單元所組成。將Jurkat T細胞培養液添加CPL共同培養後，可刺激該細胞大量產生細胞激素IL-2，顯示CPL具有調節免疫機能之潛力。

Lectins are carbohydrate recognizing proteins which prevanlently exist in most, if not all, living organisms. For a long time, plant lectins were commonly perceived as ‘antinutrients’, mainly due to their adverse effects of causing non-pathogenic food-borne poisoning when not properly cooked before consumption. However, recent studies exhibited that several lectins have been found to possess anticancer properties and showed promising potential as anticancer agents.This study provides a new strategy to detect the specific carbohydrate binding capability of lectins. A sugar-polymer based enzyme-linked adsorbent assay was established by applying different monosaccharide-polyacrylamide conjugates, including D-mannose, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine and L-fucose, as capturing agents for screening lectins in biological samples. Four model lectins, concanavalin A (Con A), wheat germ agglutinin (WGA), soybean agglutinin (SBA) and Ulex europaeus agglutinin I (UEA I), were employed as the comparative lectins against each corresponding sugar. The results suggested that this assay is more sensitive than the conventional hemagglutinating methods. On the screening of specific carbohydrate binding capability from 29 plant materials, a specific N-acetyl-D-galactosamine (GalNAc) binding capability was observed in the crude extracts of papaya (Carica papaya) seeds. The GalNAc specific binding protein was subsequently isolated and designated as CPL (C. papaya lectin). Purification of the lectin involved ammonium sulfate fractionation and DEAE anion exchange and repeated gel filtration chromatography. Inhibition of CPL causing hemagglutination on human erythrocytes showed that the lectin shows specificity to GalNAc and lactose. Surface plasmon resonance further revealed that the lectin possesses high specificity toward GalNAc with a dissociation constant of 5.5 × 10^-9 M. The lectin is composed of 38- and 40- kDa subunits with molecular mass of ~804 kDa estimated by size-exclusion high-performance liquid chromatography. Incubation of CPL with Jurkat T cells showed significant induction of IL-2 cytokine, which suggests that CPL has potent immunomodulatory effects on immune cells.

摘要..................................................ii
Abstract..............................................iii
目錄..................................................iv
圖目錄................................................vii
表目錄................................................viii
縮寫表................................................ix
第一章、研究動機......................................1
第二章、研究背景與文獻整理............................2
第2-1節、醣生物學(Glycobiology)簡介...................2
第2-2節、Lectin簡介...................................6
一、定義範圍..........................................6
二、來源與分類........................................9
三、生理活性與機能性相關研究..........................22
第2-3節、Lectin之檢測方法.............................27
第2-4節、實驗設計大綱.................................28
第三章、Lectin新檢測方法之建立........................29
第3-1節、前言.........................................30
第3-2節、材料與方法...................................31
一、 試驗材料與試劑...................................31
二、 表面結合特定醣聚合物之酵素聯結吸附分析法基本操作流程..............................31
三、 特定醣類聚丙烯胺聚合物(Sugar-PAAs)之表面吸附程度探討................................32
四、 建立對照標準Lectin分析檢量線.....................34
五、 對照Lectin之非特異性醣結合交互分析...............34
六、 Lectin與醣聚合物交互作用之游離醣類競爭抑制.......34
七、 血液凝集活性分析方法.............................35
第3-3節、結果.........................................36
一、 Sugar-PAAs之表面吸附程度探討.....................36
二、 建立標準曲線及可分析濃度範圍.....................38
三、 對照Lectin之非特異性醣結合交互分析...............40
四、 Lectin與醣聚合物交互作用之游離醣競爭抑制.........42
五、 檢測極限與靈敏度之探討...........................45
第3-4節、討論.........................................47
第四章、生物材料中新穎Lectin之篩選....................49
第4-1節、前言與研究目的...............................50
第4-2節、材料與方法...................................51
一、 試驗材料.........................................51
二、 樣品前處理與分析.................................51
三、 篩選試驗：以最適化之酵素聯結吸附分析法檢測可與特定醣基結合之食材萃取液......................................51
第4-3節、結果與討論...................................53
一、 以酵素聯結吸附分析篩選萃取液中具特定單醣結合之能力 .............................................53
二、 篩選結果之綜合比較與探討.........................57
第五章、木瓜種籽中對N乙醯半乳糖胺專一性結合Lectin之分離純化與生化性質研究........................................61
第5-1節、前言.........................................62
第5-2節、材料與方法...................................64
一、 試驗材料與試劑...................................64
二、 木瓜種籽前處理與蛋白質萃取.......................64
三、 木瓜種籽萃取物劃分與親醣蛋白之分離純化...........64
四、 純化木瓜籽Lectin之原態分子量評估：分子篩高效液相層析法 .............................................66
五、 純化木瓜籽Lectin之醣類專一性血球凝集抑制試驗.....66
六、 表面電漿共振系統測定木瓜籽Lectin對N-乙醯基半乳糖胺之親和動力學..............................................66
七、 木瓜籽Lectin對人類Jurkat T細胞與THP-1單核球細胞之細胞毒性與誘導細胞激素分泌之影響............................67
第5-3節、試驗結果.....................................69
一、 木瓜籽初步萃取與前處理...........................69
二、 陰離子交換管柱層析...............................69
三、 膠體過濾管柱層析.................................71
四、 純化之木瓜籽Lectin之醣類專一性血球凝集抑制.......76
五、 表面電漿共振方法探討木瓜籽Lectin對N-乙醯基半乳糖胺之親和動力學..............................................78
六、 木瓜籽Lectin對人類Jurkat T細胞與THP-1單核球細胞之細胞毒性與誘導細胞激素分泌之影響............................80
第5-4節、討論.........................................83
一、 分離方法探討.....................................83
二、 分子量與結構探討.................................84
三、 醣類專一性與親和動力學探討.......................85
四、 生理活性與免疫調節機能探討.......................87
第六章、結論..........................................88
參考文獻 .............................................89
附錄..................................................100
一、 本研究所使用之儀器設備...........................100
二、 各項緩衝液或溶液調配方法.........................102
三、 SDS-PAGE分析.....................................102
四、 相關著作.........................................106

Adar, R., Moreno, E., Streicher, H., Karlsson, K. A., Angstrom, J., & Sharon, N. (1998). Structural features of the combining site region of Erythrina corallodendron lectin: Role of tryptophan 135. Protein Science, 7, 52-63.
Alvarez, R. A., & Blixt, O. (2006). Identification of ligand specificities for glycan-binding proteins using glycan arrays. Methods in Enzymology, 415, 292-310.
Ashwell, G., & Harford, J. (1982). Carbohydrate-specific receptors of the liver. Annual Review of Biochemistry, 51, 531-554.
Baxevanis, C. N., Voutsas, I. F., Soler, M. H., Gritzapis, A. D., Tsitsilonis, O. E., Stoeva, S., Voelter, W., Arsenis, P., & Papamichail, M. (1998). Mistletoe lectin I-induced effects on human cytotoxic lymphocytes. I. Synergism with IL-2 in the induction of enhanced LAK cytotoxicity. Immunopharmacology and Immunotoxicology, 20, 355-372.
Bhattacharyya, L., Fant, J., Lonn, H., & Brewer, C. F. (1990). Binding and precipitating activities of Lotus tetragonolobus isolectins with L-fucosyl oligosaccharides. Formation of unique homogeneous cross-linked lattices observed by electron microscopy. Biochemistry, 29, 7523-7530.
Bies, C., Lehr, C. M., & Woodley, J. F. (2004). Lectin-mediated drug targeting: history and applications. Advanced Drug Delivery Reviews, 56, 425-435.
Bohlool, B. B., & Schmidt, E. L. (1976). Immunofluorescent polar tips of Rhizobium japonicum: possible site of attachment or lectin binding. The Journal of Bacteriology, 125, 1188-1194.
Bowles, D. J., & Pappin, D. J. (1988). Traffic and assembly of concanavalin A. Trends in Biochemical Sciences, 13, 60-64.
Boyd, W. C., & Shapleigh, E. (1954). Specific Precipitating Activity of Plant Agglutinins (Lectins). Science, 119, 419.
Bryan, M. C., Plettenburg, O., Sears, P., Rabuka, D., Wacowich-Sgarbi, S., & Wong, C. H. (2002). Saccharide display on microtiter plates. Chemistry and Biology, 9, 713-720.
Chan, H. T., Heu, R. A., Tang, C. S., Okazaki, E. N., & Ishizaki, S. M. (1978). Composition of papaya seeds. Journal of Food Science, 43, 255-256.
Cioci, G., Mitchell, E. P., Gautier, C., Wimmerova, M., Sudakevitz, D., Perez, S., Gilboa-Garber, N., & Imberty, A. (2003). Structural basis of calcium and galactose recognition by the lectin PA-IL of Pseudomonas aeruginosa. FEBS Lett, 555, 297-301.
Cooper, D. N., Boulianne, R. P., Charlton, S., Farrell, E. M., Sucher, A., & Lu, B. C. (1997). Fungal galectins, sequence and specificity of two isolectins from Coprinus cinereus. Journal of Biological Chemistry, 272, 1514-1521.
Crocker, P. R., & Varki, A. (2001). Siglecs, sialic acids and innate immunity. Trends in Immunology, 22, 337-342.
Davies, F. E., Raje, N., Hideshima, T., Lentzsch, S., Young, G., Tai, Y. T., Lin, B., Podar, K., Gupta, D., Chauhan, D., Treon, S. P., Richardson, P. G., Schlossman, R. L., Morgan, G. J., Muller, G. W., Stirling, D. I., & Anderson, K. C. (2001). Thalidomide and immunomodulatory derivatives augment natural killer cell cytotoxicity in multiple myeloma. Blood, 98, 210-216.
Depierreux, C., Kang, H. C., Guerin, B., Monsigny, M., & Delmotte, F. (1991). Characterization of an Agrobacterium tumefaciens lectin. Glycobiology, 1, 643-649.
Diaz, C. L., Spaink, H. P., & Kijne, J. W. (2000). Heterologous rhizobial lipochitin oligosaccharides and chitin oligomers induce cortical cell divisions in red clover roots, transformed with the pea lectin gene. Molecular Plant-Microbe Interactions, 13, 268-276.
Drickamer, K. (1988). Two Distinct Classes of Carbohydrate-Recognition Domains in Animal Lectins. Journal of Biological Chemistry, 263, 9557-9560.
Ettlinger, M. G., & Hodgkins, J. E. (1956). The Mustard Oil of Papaya Seed. The Journal of Organic Chemistry, 21, 204-205.
Etzler, M. E. (2000). Plant Lectins. In: B. Ernst, G. W. Hart, & P. Sinay, Carbohydrates in Chemistry and Biology, vol. 4 Lectins and Saccharide Biology (pp. 535-548). Weinheim, Germany: WILEY-VCH.
Feizi, T., Fazio, F., Chai, W., & Wong, C. H. (2003). Carbohydrate microarrays - a new set of technologies at the frontiers of glycomics. Current Opinion in Structural Biology, 13, 637-645.
Freed, D. L. J. (1999). Do dietary lectins cause disease? The evidence is suggestive - and raises interesting possibilities for treatment. British Medical Journal, 318, 1023-1024.
Fuster, M. M., & Esko, J. D. (2005). The sweet and sour of cancer: Glycans as novel therapeutic targets. Nature Reviews Cancer, 5, 526-542.
Gull, I., Wirth, M., & Gabor, F. (2007). Development of a sensitive and reliable ELISA for quantification of wheat germ agglutinin. Journal of Immunological Methods, 318, 20-29.
Gabius, H. J. (2004). The sugar code in drug delivery. Advanced Drug Delivery Reviews, 56, 421-424.
Gabius, H. J., Andre, S., Kaltner, H., & Siebert, H. C. (2002). The sugar code: functional lectinomics. Biochimica et Biophysica Acta, 1572, 165-177.
Gabius, H. J., Siebert, H. C., Andre, S., Jimenez-Barbero, J., & Rudiger, H. (2004). Chemical biology of the sugar code. CHEMBIOCHEM, 5, 740-764.
Gabor, F., Bogner, E., Weissenboeck, A., & Wirth, M. (2004). The lectin-cell interaction and its implications to intestinal lectin-mediated drug delivery. Advanced Drug Delivery Reviews, 56, 459-480.
Goldstein, I. J., Murphy, L. A., & Ebisu, S. (1977). Lectins as Carbohydrate-Binding Proteins. Pure and Applied Chemistry, 49, 1095-1103.
Goldstein, I. J., & Poretz, R. D. (1986). Isolation, physicochemical characterization and carbohydrate-binding specificity of lectins. In: I. E. Liener, N. Sharon, & I. J. Goldstein, The Lectins: Properties, Functions and Applications in Biology and Medicine (pp. 35-247). Orlando, FL: Academic Press.
Gonz''Alez De Mej''Ia, E., & Prisecaru, V. I. (2005). Lectins as bioactive plant proteins: A potential in cancer treatment. Critical Reviews in Food Science and Nutrition, 45, 425-445.
Gupta, D., Bhattacharyya, L., Fant, J., Macaluso, F., Sabesan, S., & Brewer, C. F. (1994). Observation of unique cross-linked lattices between multiantennary carbohydrates and soybean lectin. Presence of pseudo-2-fold axes of symmetry in complex type carbohydrates. Biochemistry, 33, 7495-7504.
Haidar, M., Seddiki, N., Gluckman, J. C., & Gattegno, L. (1992). Carbohydrate binding properties of the envelope glycoproteins of human immunodeficiency virus type 1. Glycoconjugate Journal, 9, 315-323.
Hakomori, S. (1996). Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism. Cancer Research, 56, 5309-5318.
Hakomori, S., & Zhang, Y. M. (1997). Glycosphingolipid antigens and cancer therapy. Chemistry and Biology, 4, 97-104.
Hamelryck, T. W., Loris, R., Bouckaert, J., Dao-Thi, M. H., Strecker, G., Imberty, A., Fernandez, E., Wyns, L., & Etzler, M. E. (1999). Carbohydrate binding, quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus. Journal of Molecular Biology, 286, 1161-1177.
Hansen, S., Holm, D., Moeller, V., Vitved, L., Bendixen, C., Reid, K. B., Skjoedt, K., & Holmskov, U. (2002). CL-46, a novel collectin highly expressed in bovine thymus and liver. J Immunol, 169, 5726-5734.
Hatakeyama, T., Murakami, K., Miyamoto, Y., & Yamasaki, N. (1996). An assay for lectin activity using microtiter plate with chemically immobilized carbohydrates. Analytical Biochemistry, 237, 188-192.
Heiny, B. M., Albrecht, V., & Beuth, J. (1998). Correlation of immune cell activities and beta-endorphin release in breast carcinoma patients treated with galactose-specific lectin standardized mistletoe extract. Anticancer Research, 18, 583-586.
Hirsch, A. M. (1999). Role of lectins (and rhizobial exopolysaccharides) in legume nodulation. Curr Opin Plant Biol, 2, 320-326.
Hori, K., Miyazawa, K., & Ito, K. (1990). Some Common Properties of Lectins from Marine-Algae. Hydrobiologia, 204, 561-566.
Kaur, K. J., Khurana, S., & Salunke, D. M. (1997). Topological analysis of the functional mimicry between a peptide and a carbohydrate moiety. The Journal of Biological Chemistry, 272, 5539-5543.
Kermanshai, R., McCarry, B. E., Rosenfeld, J., Summers, P. S., Weretilnyk, E. A., & Sorger, G. J. (2001). Benzyl isothiocyanate is the chief or sole anthelmintic in papaya seed extracts. Phytochemistry, 57, 427-435.
Kilpatrick, D. C. (2002). Animal lectins: a historical introduction and overview. Biochim Biophys Acta, 1572, 187-197.
Kilpatrick, D. C., Pusztai, A., Grant, G., Graham, C., & Ewen, S. W. B. (1985). Tomato lectin resists digestion in the mammalian alimentary canal and binds to intestinal villi without deleterious effects. FEBS Letters, 185, 299-305.
Krogfelt, K. A., Bergmans, H., & Klemm, P. (1990). Direct evidence that the FimH protein is the mannose-specific adhesin of Escherichia coli type 1 fimbriae. Infect Immun, 58, 1995-1998.
Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
Lehr, C. M., & Gabor, F. (2004). Lectins and glycoconjugates in drug delivery and targeting. Advanced Drug Delivery Reviews, 56, 419-420.
Lis, H., & Sharon, N. (1998). Lectins: Carbohydrate-Specific Proteins That Mediate Cellular Recognition. Chemical Reviews, 98, 637-674.
Liu, F. T., & Rabinovich, G. A. (2005). Galectins as modulators of tumour progression. Nature Reviews Cancer, 5, 29-41.
Minko, T. (2004). Drug targeting to the colon with lectins and neoglycoconjugates. Advanced Drug Delivery Reviews, 56, 491-509.
Mody, R., Joshi, S., & Chaney, W. (1995). Use of Lectins As Diagnostic and Therapeutic Tools for Cancer. Journal of Pharmacological and Toxicological Methods, 33, 1-10.
Mojica-Henshaw, M. P., Francisco, A. D., de Guzman, F., & Tigno, X. T. (2003). Possible immunomodulatory actions of Carica papaya seed extract. Clinical Hemorheology and Microcirculation, 29, 219-229.
Nachbar, M. S., & Oppenheim, J. D. (1980). Lectins in the United-States diet - A survey of lectins in commonly consumed foods and a review of the literature. American Journal of Clinical Nutrition, 33, 2338-2345.
Nadesalingam, J., Dodds, A. W., Reid, K. B. M., & Palaniyar, N. (2005). Mannose-binding lectin recognizes peptidoglycan via the N-acetyl glucosamine moiety, and inhibits ligand-induced proinflammatory effect and promotes chemokine production by macrophages. Journal of Immunology, 175, 1785-1794.
Nakamura, S., Ikegami, A., Matsumura, Y., Nakanishi, T., & Nomura, K. (2002). Molecular cloning and expression of the mannose/glucose specific lectin from Castanea crenata cotyledons. Journal of Biochemistry, 131, 241-246.
Nakamura, Y., Yoshimoto, M., Murata, Y., Shimoishi, Y., Asai, Y., Park, E. Y., & Sato, K. (2007). Papaya seed represents a rich source of biologically active isothiocyanate. Journal of Agricultural and Food Chemistry, 55, 4407-4413.
National_Cancer_Institute (2004). Selected Vegetables/Sun''s Soup (PDQR). National Cancer Institute.
Nilsson, C. L. (2007). Lectins: Analytical Technologies. Amsterdam, The Netherlands: Elsevier BV
Ohno, Y., Naganuma, T., Ogawa, T., & Muramoto, K. (2006). Effect of lectins on the transport of food factors in Caco-2 cell monolayers. Journal of Agricultural and Food Chemistry, 54, 548-553.
Oldenburg, K. R., Loganathan, D., Goldstein, I. J., Schultz, P. G., & Gallop, M. A. (1992). Peptide ligands for a sugar-binding protein isolated from a random peptide library. Proceedings of the National Academy of Sciences of the United States of America, 89, 5393-5397.
Olsen, L. R., Dessen, A., Gupta, D., Sabesan, S., Sacchettini, J. C., & Brewer, C. F. (1997). X-ray Crystallographic Studies of Unique Cross-Linked Lattices between Four Isomeric Biantennary Oligosaccharides and Soybean Agglutinin. Biochemistry, 36, 15073-15080.
Omori-Satoh, T., Yamakawa, Y., & Mebs, D. (2000). The antihemorrhagic factor, erinacin, from the European hedgehog (Erinaceus europaeus), a metalloprotease inhibitor of large molecular size possessing ficolin/opsonin P35 lectin domains. Toxicon, 38, 1561-1580.
Park, W. b., Lyu, S. Y., Kim, J. H., Choi, S. H., Chung, H. K., Ahn, S. H., Hong, S. Y., Yoon, T. J., & Choi, M. J. (2001). Inhibition of tumor growth and metastasis by Korean mistletoe lectin is associated with apoptosis and antiangiogenesis. Cancer biotherapy & radiopharmaceuticals, 16, 439-447.
Passera, C., & Spettoli, P. (1981). Chemical-composition of papaya seeds. Qualitas Plantarum-Plant Foods for Human Nutrition, 31, 77-83.
Peumans, W. J., Hause, B., & Van Damme, E. J. (2000). The galactose-binding and mannose-binding jacalin-related lectins are located in different sub-cellular compartments. FEBS Letters, 477, 186-192.
Peumans, W. J., & Van Damme, E. J. (1995). Lectins as plant defense proteins. Plant Physiology, 109, 347-352.
Peumans, W. J., & Vandamme, E. J. M. (1995). Lectins as Plant Defense Proteins. Plant Physiology, 109, 347-352.
Pryme, I. F., Bardocz, S., Pusztai, A., & Ewen, S. W. (2006). Suppression of growth of tumour cell lines in vitro and tumours in vivo by mistletoe lectins. Histology and Histopathology, 21, 285-299.
Pusztai, A. (1991). Plant lectins (p. 263): Cambridge University Press.
Pusztai, A., Ewen, S. W., Grant, G., Peumans, W. J., van Damme, E. J., Rubio, L., & Bardocz, S. (1990). Relationship between survival and binding of plant lectins during small intestinal passage and their effectiveness as growth factors. Digestion, 46 Suppl 2, 308-316.
Rudiger, H., & Gabius, H. J. (2001). Plant lectins: Occurrence, biochemistry, functions and applications. Glycoconjugate Journal, 18, 589-613.
Rabinovich, G. A., & Toscano, M. A. (2009). Turning ''sweet'' on immunity: galectin-glycan interactions in immune tolerance and inflammation. Nature Reviews Immunology, 9, 338-352.
Rizzi, C., Galeoto, L., Zoccatelli, G., Vincenzi, S., Chignola, R., & Peruffo, A. D. B. (2003). Active soybean lectin in foods: quantitative determination by ELISA using immobilised asialofetuin. Food Research International, 36, 815-821.
Rogers, D. J., & Fish, B. C. (1991). Marine algal lectins. In: D. C. Kilpatrick, E. van Driessche, & T. C. Bog-Hansen, Lectin Reviews, vol. 1 (pp. 129-142). St. Louis MO: Sigma Chemical Co.
Satoh, A., Fukui, E., Yoshino, S., Shinoda, M., Kojima, K., & Matsumoto, I. (1999). Comparison of methods of immobilization to enzyme-linked immunosorbent assay plates for the detection of sugar chains. Analytical Biochemistry, 275, 231-235.
Shannon, L. M., Hankins, C. N., & Strosberg, A. D. (1981). Enzymatic phytohemagglutinins: Their relation to ''classic'' legume phytohemagglutinins. In: T. C. Bog-Hansen, & E. van Driessche, Lectins─Biology, Biochemistry, Clinical Biochemistry, vol. 1 (pp. 81-91 ). Berlin: de Gruyter.
Sharma, R., van Damme, E. J. M., Peumans, W. J., Sarsfield, P., & Schumacher, U. (1996). Lectin binding reveals divergent carbohydrate expression in human and mouse Peyer''s patches. Histochemistry and Cell Biology, 105, 459-465.
Sharma, V., Srinivas, V. R., Adhikari, P., Vijayan, M., & Surolia, A. (1998). Molecular basis of recognition by Gal/GalNAc specific legume lectins: influence of Glu 129 on the specificity of peanut agglutinin (PNA) towards C2-substituents of galactose. Glycobiology, 8, 1007-1012.
Sharon, N. (2007). Lectins: Carbohydrate-specific reagents and biological recognition molecules. Journal of Biological Chemistry, 282, 2753-2764.
Sharon, N., & Lis, H. (2002). How proteins bind carbohydrates: Lessons from legume lectins. Journal of Agricultural and Food Chemistry, 50, 6586-6591.
Sharon, N., & Lis, H. (2003). Detection, occurence and isolation. Lectins (pp. 33-61). Dordrecht, The Netherlands: Springer.
Sharon, N., & Lis, H. (2004). History of lectins: from hemagglutinins to biological recognition molecules. Glycobiology, 14, 53r-62r.
Silva, F. P., Jr., Alexandre, G. M., Ramos, C. H., & De-Simone, S. G. (2008). On the quaternary structure of a C-type lectin from Bothrops jararacussu venom - BJ-32 (BjcuL). Toxicon, 52, 944-953.
Smart, J. D. (2004). Lectin-mediated drug delivery in the oral cavity. Advanced Drug Delivery Reviews, 56, 481-489.
So, L. L., & Goldstein, I. J. (1967). Protein-Carbohydrate Interaction .9. Application of Quantitative Hapten Inhibition Technique to Polysaccharide-Concanavalin A Interaction . Some Comments on Forces Involved in Concanavalin A-Polysaccharide Interaction. Journal of Immunology, 99, 158-.
Stillmark, H. (1888). Ueber Ricin, ein giftiges Ferment aus den Samen von Ricinus comm. L. und einigen anderen Euphorbiaceen. MD Thesis, Kaiserliche Universitat, Dorpat. Schnakenburg''s Buchdruckerei.
Sun, A. S., Ostadal, O., Ryznar, V., Dulik, I., Dusek, J., Vaclavik, A., Yeh, H. C., Hsu, C., Bruckner, H. W., & Fasy, T. M. (1999). Phase I/II study of stage III and IV non-small cell lung cancer patients taking a specific dietary supplement. Nutrition and Cancer, 34, 62-69.
Suzuki, T., Amano, Y., Fujita, M., Kobayashi, Y., Dohra, H., Hirai, H., Murata, T., Usui, T., Morita, T., & Kawagishi, H. (2009). Purification, characterization, and cDNA cloning of a lectin from the mushroom Pleurocybella porrigens. Bioscience, Biotechnology, and Biochemistry, 73, 702-709.
Tang, C. S. (1973). Localization of benzyl glucosinolate and thioglucosidase in Carica-papaya fruit. Phytochemistry, 12, 769-773.
Tripathi, S., & Maiti, T. K. (2005). Immunomodulatory role of native and heat denatured agglutinin from Abrus precatorius. International Journal of Biochemistry and Cell Biology, 37, 451-462.
Tung, T. C. (1998). Sword bean (Canavalia gladiata) and Linzhi. Taipei: Yuanchih Publishing.
Van Damme, E. J. M., Peumans, W. J., Barre, A., & Rouge, P. (1998). Plant lectins: A composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles. Critical Reviews in Plant Sciences, 17, 575-692.
Van Wauwe, J. P., Loontiens, F. G., & De Bruyne, C. K. (1975). Carbohydrate binding specificity of the lectin from the pea (Pisum sativum). Biochimica Et Biophysica Acta-Biomembranes, 379, 456-461.
Vasconcelos, I. M., & Oliveira, J. T. A. (2004). Antinutritional properties of plant lectins. Toxicon, 44, 385-403.
Vasta, G. R. (1992). Invertebrate lectins: distribution, synthesis, molecular biology and function. In: H. J. Allen, & E. C. Kisailus, Glycoconjugates (pp. 593-634). New York: Marcel Dekker.
Vincenzi, S., Zoccatelli, G., Perbellini, F., Rizzi, C., Chignola, R., Curioni, A., & Peruffo, A. D. B. (2002). Quantitative Determination of Dietary Lectin Activities by Enzyme-Linked Immunosorbent Assay Using Specific Glycoproteins Immobilized on Microtiter Plates. Journal of Agricultural and Food Chemistry, 50, 6266-6270.
Vitale, A., & Chrispeels, M. J. (1992). Sorting of proteins to the vacuoles of plant cells. Bioessays, 14, 151-160.
Walker, J. R., Nagar, B., Young, N. M., Hirama, T., & Rini, J. M. (2004). X-ray crystal structure of a galactose-specific C-type lectin possessing a novel decameric quaternary structure. Biochemistry, 43, 3783-3792.
Wang, H. X., Liu, W. K., Ng, T. B., Ooi, V. E. C., & Chang, S. T. (1996). The immunomodulatory and antitumor activities of lectins from the mushroom Tricholoma mongolicum. Immunopharmacology, 31, 205-211.
Wang, T.-H., Lee, M.-H., & Su, N.-W. (2009). Screening of lectins by an enzyme-linked adsorbent assay. Food Chemistry, 113, 1218-1225.
Wiley, D. C., & Skehel, J. J. (1987). The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annual Review of Biochemistry, 56, 365-394.
Woodley, J. F., & Naisbett, B. (1988). The potential of Lectins for delaying the intestinal transit of drugs. In: Proceedings of International Symposium of Controlled Release of Bioactive Materials, vol. 15 (pp. 125-126).
Yamaguchi, Y. (2000). Lecticans: organizers of the brain extracellular matrix. Cellular and Molecular Life Sciences, 57, 276-289.
Yoon, T. J., Yoo, Y. C., Choi, O. B., Do, M. S., Kang, T. B., Lee, S. W., Azuma, I., & Kim, J. B. (1995). Inhibitory effect of Korean mistletoe (Viscum album coloratum) extract on tumour angiogenesis and metastasis of haematogenous and non-haematogenous tumour cells in mice. Cancer Letters, 97, 83-91.
Zhang, S., Cordon-Cardo, C., Zhang, H. S., Reuter, V. E., Adluri, S., Hamilton, W. B., Lloyd, K. O., & Livingston, P. O. (1997a). Selection of tumor antigens as targets for immune attack using immunohistochemistry: I. Focus on gangliosides. International Journal of Cancer, 73, 42-49.
Zhang, S., Zhang, H. S., Cordon-Cardo, C., Reuter, V. E., Singhal, A. K., Lloyd, K. O., & Livingston, P. O. (1997b). Selection of tumor antigens as targets for immune attack using immunohistochemistry: II. Blood group-related antigens. International Journal of Cancer, 73, 50-56.
莊榮輝 (2005). 酵素化學實驗. 台北市, 台灣: 國立台灣大學.