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研究生:吳萬財
論文名稱:利用FusionProtein-Thioredoxin增加雞半胱胺酸蛋白酶抑制劑在大腸桿菌中之表現量及對抑制魚漿解膠之效果
論文名稱(外文):Enhanced expression of chicken cystatin escherichia coli AD494(DE3)pLysS using thioredoxin as fusion protein and its preventive effect on surimi gel softening
指導教授:江善宗
學位類別:碩士
校院名稱:國立海洋大學
系所名稱:食品科學系
學門:農業科學學門
學類:食品科學類
論文種類:學術論文
論文出版年:2002
畢業學年度:90
語文別:中文
中文關鍵詞:雞半胱胺酸蛋白酶抑制劑硫氫蛋白酶抑制劑魚漿解膠
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本研究將N端接有 thioredoxin(trx) 之 chicken cystatin cDNA接合於 pET-23a(+) expreesion vector 後,轉形入E. coli AD494(DE3) pLysS 表現宿主中表現。經isopropyl-β-D-thiogalactopyanoside誘導後,可於E. coli的cytoplasm中大量表現出可溶之trx-cystatin。與未融合thioredoxin之recombinant cystatin比較,結果發現藉由thioredoxin fusion protein可以提高38.7﹪可溶性trx-cystatin的抑制活性。此trx-cystatin經由簡單的加熱及Sephacryl S-100 HR膠過濾管柱層析而純化。其分子量如預期為29 kDa,包含recombinant thioredoxin (16 kDa)及chicken cystatin (13 kDa)。該trx-cystatin之表現與recombinant cystatin及chicken cystatin相似,具有良好的熱安定性及抑制 papain-like cysteine proteinases 之活性。將此抑制劑添加於鯖魚魚漿,發現具有抑制魚漿中內生性組織蛋白酶活性,同時亦達到抑制魚漿解膠之效果。
The DNA encoding chicken lung cystatin was ligated into thioredoxin-pET 23a+ expression vector and transformed into Escherichia coli AD494(DE3)pLysS. High level of soluble recombinant thioredoxin-cystatin (trx-cystatin) was expressed in the cytoplasm of E. coli transformant. Comparing with recombinant cystatin (trx-free), a 38.7% increase of inhibitory activity in soluble fraction was achieved by introducing trx fusion protein. The trx-cystatin was purified to electrophoretical homogeneity by 3 min heating at 90°C and Sephacryl S-100 HR chromatography. The molecular mass of trx-cystatin was 29 kDa, which was the expected size composing of recombinant trx (16 kDa) and chicken cystatin (13 kDa). The purified trx-cystatin behaved as a thermal stable and papain-like proteinase inhibitor comparable to either recombinant or natural chicken cystatins. The inhibitor could inhibit the gel softening of mackerel surimi.
Keywords: Chicken cystatin; Cysteine proteinase inhibitor; thioredoxin; pET 23a+; E. coli AD494(DE3)pLysS; Over expression.
目錄
頁數
中文摘要………………………………………………………………....…1
英文摘要………………………………………………………...…….…....2
壹、研究動機與目的………………………………………………….…....3
貳、文獻整理……………………………………………………….……....5
一、硫氫蛋白酶之分類………………………………..……….…….…5
二、硫氫蛋白酶的分佈與存在位置……………………………….…..7
A、溶素體硫氫蛋白…………………………………..……....…7
B、鈣肽酶……………………………………………………….….8
三、組織蛋白酶L之基質特異性……………………………..…….…9
A、組織蛋白酶L對肌肉蛋白之水解情形…………….….……...9
B、組織蛋白酶L對胜肽鍵之選擇性水解部位……...…………..11
四、蛋白酶對煉製品膠強度之影響………………………………….12
五、抑制劑對魚漿解膠之影響……………………………………….13
A、絲胺酸蛋白酶(Serine proteinases)抑制劑……………………13
B、硫氫蛋白酶(Cysteine proteinases)抑制劑…………………….13
六、組織蛋白酶L和B的特異性合成抑制劑………………..…….14
七、硫氫蛋白酶的天然抑制劑……………..………………..………15
A、Calpastatin…………….……………………………………….15
B、Cystatin………………………………………………..………17
a. Stefins………………………...…………...…...……………..18
b. Cystatins…………………………………..………………….19
c. Kininogens…………………………..…...………...…………20
d. Oryzacystatins……………………………………...…………21
八、硫氫蛋白酶天然抑制劑之生化特性…………………………….22
參、實驗設計………………………………..……………….……………26
肆、實驗材料……………………………………………………….……..26
一、菌種…………………………………………………….…..…….26
二、質體……………………………………………………………….26
三、原料……………………………….………………………………26
四、藥品…………………………………………….………..….……26
五、儀器………………………….……………….……………………27
伍、實驗方法…………………………………………….……..………..29
一、雞肺硫氫蛋白酶抑制劑基因之選殖………………..………..……..29
A、組織細胞(Tissue cell) total RNA的萃取….……….……..…29
B、反轉錄作用(Reverse transcription)….…………….……..…..30
C、硫氫蛋白酶抑制劑基因專一性引子的設計……..……….…..30
D、聚合酶鏈鎖反應(Polymerase chain reaction )………..……...31
E、重組硫氫蛋白酶抑制劑之基因.…………………..…………..31
a. DNA電泳的製備……………………………..………....…31
b. PCR反應後產物的純化…………………………..….…..32
c. TA-Cloning….……………………………………...….……32
d. E.coli Strain通透性細胞的製備………………..….……...32
e. 質體轉形入E.coli Top 10F’通透性細胞………..….……32
f. 重組硫氫蛋白酶抑制劑之質體DNA的抽取…...…….…..33
g. 限制酶作用…………………………………..…………….34
h. Phenol/Chloroform萃取…………………….………..…...34
i. 接合作用……………………………………… …...…..…34
j. 融合蛋白質基因……………………………………..…...34
k. 質體轉形入E.coli AD494(DE3)pLysS通透性細胞.…...35
二、Trx-Cystatin基因的大量表現………………………….…….…35
三、Trx-Cystatin的純化………………………………….……….…36
A、Trx-Cystatin的抽取………………………………….………36
B、加熱反應…………………………………………….……..…36
C、Sephacryl S-100 HR膠過濾管柱層析……………………..…36
D、Enterokinase作用……………………………………………..37
E、FPLC Superdex 75 (1.0´30cm)膠過濾管柱層析……………..37
四、活性測定………………………………………………..………..37
A、以E-64 滴定Papain, Cathepsin B 和Cathepsin L之有效濃度……….………………………………………………...……….37
B、Cystatin抑制活性的測定…………………………………....38
五、耐熱性研究…………………………………………………...….38
六、蛋白質的定量………………………………………………..…..39
七、Trx-cystatin在魚漿上之應用……………………….……..…….39
A、冷凍魚漿之製備………………………………………………39
B、探討trx-cystatin添加對煉製品解膠之影響…………………39
C、膠強度的測定…………………………………………………39
D、電泳分析……………………………………………..…..……40
陸、結果與討論…………………………………………………..…….…41
A、pET-23a(+)-Trx-cystatin expression vector之構築及選殖…………………………………………...…………...…...41
B、Trx-cystatin基因之誘導與大量表現………………………...42
C、Trx-cystatin之純化…………………………….………...…...43
D、Trx-cystatin之活性分析…………………………………...…44
E、Trx-cystatin之熱安定性分析……………………………...….45
F、添加Trx-cystatin對鯖魚魚漿解膠之抑制影響情形….…..…45
柒、結論…….……………………………………………………………..46
捌、參考文獻………………………………………………………………47
圖表目錄
頁數
表一、E. coli AD494(DE3)pLysS所表現出之trx-cystatin之純化……..53
表二、Trx- cystatin對冷凍鯖魚魚漿煉製品膠強度之影響…………….54
圖一、雞肺臟細胞之total cDNA經PCR反應之洋菜膠電泳圖……….55
圖二、Trx-pET-23a(+)-cystatin表現載體之構築與表現流程圖………..56
圖三、Cystatin-pGEM-T Easy vector之洋菜膠電泳分析圖…………….57
圖四、Trx-pET-23a(+)-cystatin表現載體之洋菜膠電泳分析圖………..58
圖五、Trx-pET23a(+)-cystatin表現載體與限制酶反應後洋菜膠電泳分析圖……………………………………………………………….…59
圖六、Trx-pET-23a(+)-cystatin表現載體之構築…………………….....60
圖七、Trx-chicken cystatin fusion protein序列之構築…………………..61
圖八、表現自E. coli AD494(DE3)pLysS之trx- cystatin在Sephacryl S-100 HR的管柱層析圖……………………………………..…..62
圖九、Trx- cystatin 之SDS-PAGE蛋白質電泳分析圖……………..…63
圖十、表現自E. coli AD494(DE3)pLysS之Trx-cystatin對木瓜酵素、鯖魚組織蛋白酶B及L之抑制活性分析圖……………………….64
圖十一、Trx- cystatin與重組雞硫氫蛋白酶抑制劑之熱安定性分析圖……………………………………………………………….…65
圖十二、Trx- cystatin 對於鯖魚魚漿解膠作用之影響電泳分析圖…....66
Abe, K. and Arai, S. 1985. Purification of a cysteine proteinase inhibitor from rice, Oryza sativa L. Japonica. Agric. Biol. Chem. 49: 3349-3350.
Abe, K., Emori, Y., Kondo, H., Arai, S. and Suzuki, K. 1988. The NH2-terminal 21 amino acid residues are not essential for the papain-inhibitory activity of oryzacystatin, a member of cystatin superfamily. J. Biol. Chem. 236: 7655-7659.
Abe, K., Emori, Y., Kondo, H., Suzuki, K. and Arai, S. 1987a. Molecular cloning of a cysteine proteinase inhibitor of rice (Oryzacystatin). J. Biol. Chem. 262 (35): 16793-16797.
Abe, K., Kondo, H., Watanabe, H., Emori, Y. and Arai, S. 1991. Oryzacystatins as the first well-defined cystatins of plant origin and their target proteinases in rice seeds. Biomed. Biochim. Acta 50: 637-641.
Abe, K.; Hiroto, K.; Arai, S. 1987b. Purification and characterization of a rice cysteine proteinase inhibitor. Agric. Biol. Chem. 51: 2763-2765.
Abe, M., Arai, S., Kato, H., and Fujimaki, M. 1980. Thiol-protease inhibitors occurring in endosperm of corn. Agric. Biol. Chem. 44: 685-686.
Abe, Y., Yasunaga, K., Kitakami, S. and Ota, T. 1995. Quality of kamaboko gels from walleye pollack frozen surimis of different grades with bovine plasma powder. Nippon Suisan Gakkaishi 61:750.
Abrahamson, M. 1994. Cystatins. Methods Enzymol. 244: 685-700.
Abrahamson, M., Barrett, A. J., Salvesen, G., and Grubb, A. 1986. Isolation of six cysteine proteinase inhibitors from human urine. Their physicochemical and enzyme kinetic properties and concentratios in biological fluids. J. Biol. Chem. 261: 11281-11289.
Abrahamson, M., Grubb, A., Olafsson, I. and Lundwall, A. 1987a. Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C. FEBS Lett. 216: 229-233.
Abrahamson, M., Mason, R. W., Hansson, H., Buttle, D.J., Grubb, A. and Ohlsson, K. 1991. Human cystatin C. role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase. Biochem. J. 273(3): 621-626.
Abrahamson, M., Olafsson, I., Palsdottir, A., Ulvsback, M., Lundwall, A., Jensson, O. and Grubb, A. 1990. Structural and expression of the human cystatin C gene. Biochem. J. 268: 287-294.
Abrahamson, M., Ritonja, A., Brown, M. A., Grubb, A., Machleidt, W. and Barrett, A. J. 1987b. Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors human cystatin c and chicken cystatin. J. Biol. Chem.262(20): 9688-9694.
Akers, C. P. and Hoff, J. E. 1980. Simutaneous formation of chymopapain inhibitor activity and cubical crystals in tomato leaves. Can. J. Bot. 58: 1000-1003.
Al-Hashimi, I., Dickinson, D. P. and Levine, M. J. 1988. Purification, molecular cloning, and sequencing of salivary cystatin SA-I. J. Biol. Chem. 263: 9381-9387.
An, H., Seymour, T. A., Wu, J. W. and Morrissey, M. T. 1994a. Assay systems and characterization of Pacific whiting (Merluccius productus) protease. J. Food Sci. 59: 277-281.
An, H., Weerasinghe, V., Seymour, T. A. and Morrissey, M. T. 1994b. Cathepsin degradation of Pacific whiting surimi proteins. J. Food Sci. 59(5): 1013-1017, 1033.
Anastasi, A., Brown, M. A., Kembhavi, A. A., Nicklin, M. J. H., Sayers, C. A., Sunter, D. C. and Barrett, A. J. 1983. Cystatin, a protein inhibitor of cysteine proteinase. Improved purification from egg white, characterization, and detection in chicken serum. Biochem. J. 211: 129-138.
Aranishi, F., Hara, K. and Ishihara, T. 1992. Purification and characterization of cathepsin H from hepatopancreas of carp Cyprinus carpio. Comp. Biochem. Physiol. 102B: 499-505.
Asada, K., Ishino, Y., Shimada, M., Shimojo, T., Endo, M., Kimizuka, F., Kato, I., Maki, M., Hatanaka, M. and Murachi, T. 1989. cDNA cloning of human calpastatin: structure comparison between human, pig, and rabbit calpastatins. J. Enzyme Inhibition. 3: 49-56.
Azaryan, A. and Galoyan, A. 1987. Human and bovine brain cathepsin L and cathepsin H: Purification, physico-chemical properties, and specificity. Neurochem. Res. 12: 207-213.
Bando, Y., Kominami, E. and Katunuma, N. 1986. Purification and tissue distribution of rat cathepsin L. J. Biochem. 100: 35-42.
Baricos, W. H., Zhou, Y., Mason, R. W. and Barrett A. J. 1988. Human Kidney cathepsin B and L. Characterization and potential role in degradation of glomerular basement membrane. Biochem. J. 252: 301-304.
Barrett, A. J. 1973. Purification and some properties of the enzyme. Biochem. J. 131: 809-822.
Barrett, A. J. 1981. Cystatin, the Egg White Inhibitor of Cysteine Proteinases. Methods in Enzymology. 80: 771-778.
Barrett, A. J. 1987. The cystatins: a new class of peptidase inhibitors. Trends Biochem. Sci. 12: 193-196.
Barrett, A. J., Fritz, H., Grubb, A., Isemura, S., Jarvinen, M., Katunuma, N., Machleidt, W., Muller-Esterl, W., Sasaki, M., and Turk, V. 1986a. Nomenclature and classi-fication of the proteins homologous with the cysteine-proteinase inhibitor chicken cystatin. Biochem. J. 236: 311-3122.
Barrett, A. J., Kembhavi, A. A., Brown, M. A., Kirschke, H., Knight, C. H., Tamai, M. and Hanada, K. 1982. L-trans-eopxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B,H and L. Biochem. J. 201: 189-198.
Barrett, A. J., Rawlings, N. D., Davies, M. E., Machleidt, W., Salvesen, G., and Turk, V. 1986b. Cysteine proteinase inhibitors of the cystatin superfamily. In Proteinase Inhibitors, Barrett, A. J. and Salvesen, G. Eds., pp 515-569, Elsevier, Amsterdam.
Baudry, M. and Lynch, G. 1980. Regulation of hippocampal glutamate receptors: evidence for involvement of a calcium-activated protease. Proc. Natl. Acad. Sci. USA. 77: 2298-2302.
Baudry, M., Bundman, M. C., Smith, E. K. and Lynch, G. S. 1981. Micromolar calcium stimulates proteolysis and glutamate binding in rat synaptic membranes. Science. 212: 937-938.
Baumgartner, B. and Chrispeels, M. J. 1976. Partial characterization of a protease inhibitor which inhibits the major endopeptidase present in the cytoledons of mung bean. Plant Physiol. 58: 1-6.
Berri, M., Venien, A., Levieux, D. and Ouali. A. 1996. Tissue distribution and characterization of a 30kDa cysteine proteinase inhibitor from bovine skeletal muscle. Comp. Biochem. Physiol. 113B: 275-279.
Berti, P. J. and Storer, A. C. 1994. Local pH-dependent conformational changes leading to proteolytic susceptibility of cystatyin C. Biochem. J. 302: 411-416.
Bjork, I. and Ylinenjarvi, K. 1989. Interaction of chicken cystatin with inactivated papains. Biochem. J. 260: 61-68.
Bjork, I., Brieditis, I., Raub-Segall, E., Pol, E., Håkansson, K. and Abrahamson, M. 1996. The importance of the second hairpin loop of cystatin C for proteinase binding. Characterization of the interaction of Trp-106 variants of the inhibitor with cysteine proteinases. Biochemistry 35: 10720-10726.
Bobek, L. A., Aguirre, A. and Levine, M. J. 1991. Human salivary cystatin S. Biochem. J. 278: 627-635.
Bode, W., Brzin, J. and Turk, V. 1985. Crystallization of chicken egg white cystatin, a low molecular weight protein inhibitor of cysteine proteinases, and preliminary X-ray diffraction data. J. Mol. Biol. 181: 331-332.
Bode, W., Engh, R., Musil, D., Laber, B., Stubbs, M., Huber, R. and Turk, V. 1990. Mechanism of interaction of cysteine proteinases and their protein inhibitors as compared to the serine proteinase-inhibitor interaction. Biol. Chem. Hoppe-Seyler. 371: 111-118
Bode, W., Engh, R., Musil, D., Thiele, U., Huber, R., Karshikov, A., Brzin, J., Kos, J., and Turk, V. 1988. The 2.0 Å X-ray crystal structure of chicken egg white aystatin and its possible mode of interaction with cysteine proteinases. EMBO J. 7(8): 2593-2599.
Bond, J. S. and Butler, P. E. 1987. Intracellular proteases. Ann. Rev. Biochem. 333-364.
Bonete, M. J., Manjon, A., Llorca, F. and Iborra, J. L. 1984. Acid proteinase activity in fish I. Comparative study of extraction of cathepsin B and D from Mujil aratus. Comp. Biochem. Physiol. 78B: 203-206.
Boulter, D. and Harvey, P. J. 1985. Accumulation, structure and utilization of tuber storage proteins with particular reference to Dioscorea rotundata. Physiol. Veg. 23: 61-74.
Brzin, J., Kopitar, M. and Turk, V. 1983. Protein inhibitors of cysteine proteinases I. Isolation and characterization of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphnuclear granulocytes. Hoppe-Seyler Z. Biol. Chem. 364: 1475-1478.
Brzin, J., Popovic, T. and Turk, V. 1984. Human cystatin, a new protein inhibitor of cysteine proteinases. Biochem. Biophys. Res. Commun. 118: 103-109.
Brzin, J.; Ritonja, A.; Popovic, T.; Turk, V. 1990. Low molecular mass protein inhibitor of cysteine proteinases from soybean. Hoppe-Seyler Z. Biol. Chem. 371: 167-170.
Calkins, C. C. and Sloane, B. F. 1995. Mammalian cysteine protease inhibitors: Biochemical properties and possible roles in tumor progression. Biol. Chem. Hoppe-Seyler 376: 71-80.
Chen, G. H.; Tang, S. J.; Chen, C. S.; Jiang, S. T. Overexpression of the soluble form of chicken cystatin in Escherichia coli and its purification. J. Agric. Food Chem. 2000, 48, 2602-2607.
Clausen, J. A. and Blest, A. D. 1996. A cysteine proteinase inhibitor on crab retina crystalline cones: purification and immunohistochemical localisation. Comp. Biochem. Physiol. 113B: 511-523.
Dalet-Fumeron, V., Guinec, N. and Pagano, M. 1991. High-performance liquid chromatographic method for the simultaneous purification of cathepsin B, H and L from human liver. J. Chromatogr. 568: 55-68.
Dayton W. R. Schollmeyer, J. V. 1980. Localization of a Ca2+-activated neutral protease in skeletal muscle. J. Cell Biol. 87: 267a.
Dayton, W. R., Schollmeyer, J. F. and Lepley, R. A. 1981. A calcium-activated protease possibly involved in myofibrillar protein turnover. Isolation of a low-calcium-requiring form of the protease. Bichim. Biophys. Acta. 659: 48-61.
DeMartino, G. N. 1981. Calcium-dependent proteolytic activity in rat liver: Identification of two proteases with different calcium requirement. Arch. Biochem. Biophys. 211: 253-257.
Dolenc, I., Turk, B., Kos, J. and Turk, V. 1996. Interaction of human cathepsins C with chicken cystatin. FEBS Letters. 392: 277-280.
Dufour, E., Obled, A., Valin, C. and Bechet, D. 1987. Purification and amino acid sequence of chicken liver cathepsin L. Biochemistry. 26: 5689-5695.
Esnard, F., Esnard, A., Faucher, D., Capony, J., Derancourt, J., Brillard, M. and Gauthier, F. 1990. Rat ctstatin C: the complete amino acid sequence reveals a site for N-glycosylation. Biol. Chem. Hoppe-Seyler 371, Suppl.: 161-166.
Funaki, J., Abe, K., Hayabuchi, H. and Arai, S. 1991. Modulating the conditioning of meat by the use of oryzacystatin, a cysteine proteinase inhibitor of rice seed origin. J. Food Biochem. 15: 253-262.
Gabrijelcic, D., Gollwitzer, R., Popovic, T., and Turk, V. 1988. Proteolytic cleavage of human fibrinogen by cathepsin B. Biol. Chem. Hoppe-Seyler 369 Suppl.: 287-292.
Gauthier, F., Moreau, T., Lalmanach, G., Brillard-Bourdet, M., Martino, M. F. D. and Juliano, L. 1993. A new, sensitive fluorogenic substrate for papain based on the sequence of the cystatin inhibitory site. Arch. Biochem. Biophys. 306: 304-308.
Green, G. D. J. and Shaw, E. 1981. Peptidyl diazomethyl ketones are specific inactivators of thiol proteinases. J. Biol. Chem. 25: 1923-1928.
Green, G. D. J., Kembhavi, A. A., Davies, M. E., and Barrett, A. J. 1984. Cystatin-like cysteine proteinase inhibitors from human liver. Biochem. J. 218: 939-946.
Grubb, A. and Lofberg, H. 1982. Human g-trace, a basic microprotein: Amino acid sequence and presence in the adenohypophysis. Proc. Natl. Acad. Sci. U.S.A. 79: 3024-3027.
Grubb, A., Lofberg, H. and Barrett, A. J. 1984. The disulphide bridge of human cystatin C (g-trace) and chicken cystatin. FEBS Lett. 170 (2): 370-374.
Haard, N. F. 1990. Enzymes from food myosystems. J. Muscle Foods 1:292.
Haard, N. F. 1992. A review of proteolytic enzymes from marine organisms and their application in the food industry. J. Aquatic Food Product Tech. 1: 17-35.
Hanada, K., Tamai, M., Yamagushi, M., Ohmura, S., Sawada, J. and Tanaka, I. 1978. Isolation and characterization of E-64, a new thiol protease inhibitor. Agric. Biol. Chem. 42: 523-528.
Hara, K., Suzumatsu, A. and Ishihara, T. 1988. Purification and characterization of cathepsin B from carp ordinary muscle. Nippon Suisan Gakkaishi. 54: 1243-1252.
Hardy, M. and Pennington, R. J. T. 1979. Separation of cathepsin B1 and related enzymes from rat skeletal muscle. Biochim. Biophys. Acta. 577: 253-266.
Hill, P. A., Buttle, D. J., Jones, S. J., Boyde, A., Murata, M. and Reynolds, J. J. 1994. Inhibition of bone resorption by selective inactivators of cysteine proteinase. J. Cell Biochem. 56: 118-130.
Hirashiki, I., Ogata, F., Yoshida, N., Makisumi, S. and Ito, A. 1990. Purification and complex formation analysis of a cysteine proteinase inhibitor (cystatin) from seeds of Wisteria floribunda. J. Biochem. 108: 604-608.
Ho, M. L., Chen, G. H. and Jiang, S. T. 2000. Effects of mackerel cathepsins L and L-like, and calpain on the degradation of mackerel surimi. Fish. Sci. 66: 558-568.
Ii, K., Hizawa, K., Nonaka, I., Sugita, H., Kominami. E. and Katunuma, N. 1986. Abnormal increases of lysosomal cysteine proteinases in rimmed vacuoles in the skeletal muscle. Am. J. Pathol. 122: 193-198.
Im, B., Kominami, E., Grube, D. and Uchiyama, Y. 1989. Immunocytochemical localization of cathepsins B and H in human pancreatic endocrine cells and insulinoma cells. Histochemistry. 93: 111-118.
Inubushi, T., Kakegawa, H., Kishino, Y. and Katunuma, N. 1994. Specific assay method for the activities of cathepsin L-type cysteine proteinases. J. Biochem. 116: 282-284.
Isemura, S., Saitoh, E. and Sanada, K. 1984b. Isolation and amino acid sequence of SAP-1, and acidic protein of human whole saliva, and sequence homology with human g-trace. J. Biochem. 96: 489-498.
Isemura, S., Saitoh, E. and Sanada, K. 1986. Characterization of a new cysteine proteinase inhibitor of human saliva, cystatin SN, which is immunologically related to cystatin S. FEBS Lett. 198: 145-149.
Isemura, S., Saitoh, E. and Sanada, K. 1987. Characterization and amino acid sequence of a new acidic cysteine proteinase inhibitor (Cystatin SA) structurally closely related to cystatin S, from human whole saliva. J. Biochem. 102: 693-704.
Isemura, S., Saitoh, E., Ito, S., Isemura, M. and Sanada, K. 1984a. Cystatin S: A cysteine proteinase inhibitor of human saliva. J. Biochem. 96: 1311-1314.
Ishida, M., Sugiyama, N., Sato, M. and Nagayama, F. 1995. Two kinds of neutral serine proteinases in salted muscle of anchovy, Engraulis japonica. Biosci. Biotech. Biochem. 59: 1107.
Ishiura, S., Sugita, H., Nonaka, I. And Imahori, K. 1980. Calcium-activated neutral protease. its localization in the myofibril, especially at the Z-band. J. Biochem. 86: 579-581.
Jarvinen, M. 1978a. Purification and some characteristics of the human epidermal SH-protease inhibitor. J. Invest. Dermatol. 72: 114-118.
Jarvinen, M., Rasanen, O., Rinne, A. 1978b. The low-molecular-weight SH-protease inhibitor in rat skin is epidermal. J. Invest. Dermatol. 71: 119-121.
Jiang, S. T., Lee, B. L., Tsao, C. Y. and Lee, J. J. 1997. Mackerel cathepsins B and L effects on thermal degradation of surimi. J. Food Sci. 62(3): 310-315.
Jiang, S. T., Lee, J. J. and Chen, H. C. 1994. Purification and characterization of cathepsin B from ordinary muscle of mackerel (Scomber australasicus). J. Agri. Food Chem. 42: 1073-1079.
Jiang, S. T.; Chen, G. H. 1998. Effect of Cathepsins B, L, L-like and Calpain on the Protein Degradation of Surimi. In Quality Attributes of Muscle Foods, Chapter 26, ACS Symposium Series 215, (ed. Xiong, Y. L. Ho, C. T. & Shahidi, F.) 393-405 (Kluwer Academic/Plenum Publishers, New York, NY).
Kakegawa, H., Nikawa, T., Tagami, K., Kamioka, H., Sumitani, K., Kawata, T., Drobnic-K, M., Lenarcic, B., Turk, V. and Katunuma, N. 1993. Participation of cathepsin L on bone resorption. FEBS Letter. 321(2,3): 247-250.
Kamphuis, I. G., Drenth, J. and Baker, E. N. 1985. Thiol proteases, comparative studies based on the high resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain. J. Mol. Biol. 182: 317-329.
Kargel, H. J., Dettmer, R., Etzold, G., Kirschke, H., Bohley, P. and Langner, J. 1980. Action of Cathepsin L on the oxidized B-chain of bovine insulin. FEBS Lett. 114(2): 257-260.
Kartasova, T., Cornelissen, B. J. C., Belt, P. and Van de Putte, P. 1987. Effects of UV, 4-NQQ and TPA on gene expression in cultured human epidermal kerationcytes. Nucleic Acids Res. 15: 5945-5962.
Kato, H., Nagasawa, S. and Iwanaga, S. 1981. HMW and LMW kininogens. Meth. Enzymol. 80: 172-198.
Katunuma, N., Towatari, T., Tamai, M. and Hanada, K. 1983. Use of new synthetic substrates for assays of cathepsin L and cathepsin B. J. Biochem. 93: 1129-1135.
Kawasaki, H., Emori, Y., Imajoh, S., Minami, Y., and Suzuki, K., Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease. J.biochem. 1989: 106,274-281.
Keilova, H. and Tomasek, V. 1974. Effect of papain inhibitor from chicken egg white on cathepsin B1. Biochim. Biophys. Acta 334: 179-186.
Kirschke, H, Langner, J., Wiederanders, B., Ansorge, S. and Bogley, P. 1977. Cathepsin L : A new proteinase from rat liver lysosomes. Eur. J. Biochem. 74: 293-301.
Kirschke, H. and Barrett, A. J. 1987. Chemistry of lysosomal proteases. In Lysosomes:Their role in protein breakdown (ed. by Glaumann H. and Ballard F. J.). pp: 193-238. Academic Press, London.
Kirschke, H. and Shaw, E. 1981. Rapid interaction of cathepsin L by Z-Phe-Phe-CHN2 and Z-Phe-Ala-CHN2. Biochem. Biophys. Res. Commun. 101: 454-458.
Kirschke, H., Kembhavi, A. A., Bohley, P. and Barrett, A. J. 1982. Action of rat liver cathepsin L on collagen and other substrates. Biochem. J. 201: 367-372.
Kishimoto, A., Kajikawa, N., Shiota, M. and Nishizuka, Y. 1983. Proteolytic activation of calcium-activated phospholipid-dependent protein kinase by calcium-dependent neutral protease. J. Biol. Chem. 258: 1156-1164.
Kishimoto, A., Kajikawa, N., Tabuchi, H., Shiota, M. and Nishizuka, Y. 1981. Calcium-dependent neutral proteases, widespread occurrence of a species of a protease active at lower concentration of calcium. J. Biochem. (Tokyo) 90: 889-892.
Kominami, E. K., Tsukahara, T., Hara, K. and Katunuma, N. 1988. Biosyntheses and processing of lysosomal cysteine proteinases in rat macrophages. FEBS Lett. 231: 225-228.
Kominami, E., Bando, Y., Ii, K., Hizawa, K. and Katunuma, N. 1984. Increases in cathepsin B and L and thiol proteinase inhibitors in muscle of dystrophic hamsters. Their localization in invading phagocytes. J. Biochem. 96: 1941-1948.
Kominami, E., Ii, K. and Katunuma, N. 1987. Activation of the intramyofibral autophagic-lysosomal system in muscular dystrophy. Am. J. Pathol. 127: 461-466.
Kondo, H., Abe, K., Nishimura, I., Watanabe, H., Emori, Y. and Arai, S. 1990. Two distinct cystatin species in rice seeds with different specificities against ctateine proteinases. Molecular cloning, expression, and biochemical studies on oryzacystatin-II J. Biol. Chem. 265: 15832-15837.
Korant, B., Towatari, T., Kelley, M., Brzin, J., Lenarcic, B. and Turk, V. 1988. Interactions between a viral protease and cystatins. Biol. Chem. Hoppe-Seyler 369 Suppl.: 281-286.
Kouzuma, Y., Kawano, K., Kimura, M., Yamasaki, N., Kadowaki, T. and Yamamoto, K. 1996. Purification, characterization, and sequencing of two cysteine proteinase inhibitors, Sca and Scb, from sunflower (Helianthus annuus) seeds. J. Biochem. 119: 1106-1113.
Krieger, T. J. and Hook, V. Y. H. 1991. Purification and characterization of a novel thiol protease involved in processing of the enkephalin precursor. J Biol. Chem. 266: 8376-8383.
Kumazawa, Y., Nakanishi, K., Yasueda, H. and Motoki, M. 1996. Purification and characterization of transglutaminase from walleye pollack liver. Fisheries Sci. 62: 959-964.
Lah, T. A., Kokalj-Kunovar, M. and Turk, V. 1990. Cysteine proteinase inhibitors in human cancerous tissues and fluids. Biol. Chem. Hoppe-Seyler. 371 Suppl. 199-203.
LaVallie, E. R., DiBlasio, E. A., Kovacic, S., Grant, K. L., Schendel, P. F. and McCoy, J. M. 1993. A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm. Biotechnology. 11(2): 187-193.
Lenarcic, B., Ritonja, A., Dolenc, I., Stoka, V., Berbic, S., Pungercar, J., Strukelj, B. and Turk, V. 1993. Pig leukocyte cysteine proteinase inhibitor (PLCPI), a new member of the stefin family. FEBS Letter. 336(2): 289-292.
Leonardi, A., Turk, B. and Turk, V. 1996. Inhibition of bovine cathepsins L and S by stefins and cystatins. Biol. Chem. Hoppe-Seyler 377: 319-321.
Liang, C., Brookhart, G., Feng, G. H., Reeck, G. R. and Kramer, K. J. 1991. Inhibition of digestive proteinases of stored grain coleoptera by oryzacystatin, a cysteine proteinase inhibiotr from rice seed. FEBS Lett. 278(2): 139-142.
Lindahl, P., Ripoll, D., Abrahamson, M., Mort, J. S. and Storer, A. C. 1994. Evidence for the interaction of valine-10 in cystatin C with the S2 subsite of cathepsin B. Biochemistry 33: 4384-4392.
Liu, D., Kanoh, S. and Niwa, E. 1996a. Effect of cysteine protease inhibitor on the setting of Alaska pollack surimi paste. Nippon Suisan Gakkaishi 62: 275-280.
Liu, D., Nowsad, A. AKM., Kanoh, S. and Niwa, E. 1996b. Effect of serine protease inhibitor on the setting of Alaska pollack surimi paste. Nippon Suisan Gakkaishi 62: 791-796.
Machleidt, W., Thiele, U., Laber, B. Assfalg-Machleidt, I. Esterl, G. W. Kos, J. Turk, V. and Bode, W. 1989. Machanism of inhibition of papain by chicken egg white cystatin: Inhibition constants of N-terminally truncated forms and cyanogen bromide fragments of the inhibitor. FEBS Lett. 243(2): 234-238.
Machleidt, W., Thiele, U., Machleidt, I. A., Forger, D. and Auerswald, E. A. 1991. Molecular mechanism of inhibition of cysteine proteinases by their protein inhibitors: Linetic studies with natural and recombinant variants of cystatins and stefins. Biomed. Biochim. Acta. 50 (4-6): 613-620.
Maki, M., Takano, E., Osawa, T., Ooi, T., Murachi, T., and Hatanaka, M., Analysis of structure-function relationship of pig calpastatin by expression of mutated cDNAs in Escherichia coli. J. Biol. Chem. 1988, 263(21): 10254-10261.
Makinodan, Y., Toyohara, H and Niwa, E. 1985. Implication of muscle alkaline protease in the textural degradation of fish meat gel. J. Food Sci. 50: 1351-1355.
Marks, N. and Berg, M. J. 1987. Rat brain cathepsin L: characterization and differentiation from cathepsin B utilizing opioid peptides. Archs. Biochem. Biophy. 259: 131-143.
Mason, R, W., Gpeen, G. D. J. and Barrett, A. J. 1985. Human liver cathepsin L. Biochem. J. 226: 233-241.
Mason, R. W., Taylor, M. A. J. and Etherington D. J. 1984. The purification and properties of cathepsin L from rabbit liver. Biochem. J. 217: 209-217.
Matsukura, U., Okitani, A., Nishimuro, T. and Kato, H. 1981. Mode of degradation of myofibrillar proteins by an endogenous protease, cathepsin L. Biochem. Biophys. Acta. 662: 41-47.
Matsumiya, M., Mochizuki, A. and Otake, S. 1989. Purification and characterization of cathepsin B from ordinary muscle of common mackerel Scomber japonicus. Nippon Suisan Gakkaishi. 55: 2185-2190.
Mellgren, R. L. 1980. Canine cardiac calcium-dependent proteases: resolution of two forms with different requirements for calcium. FEBS Lett. 109: 129-133.
Menard, R., Carmona, E., Plouffe, C., Dieter, B., Konishi, Y., Lefebvre, J. and Storer, A. C. 1993. The specificity of the S1’ subsite of cysteine proteases. FEBS Lett. 328(1,2): 107-110.
Mikami, M., Whiting, A. H., Taylor, M. A. J., Maciewicz, R. A. and Etherington, D. J. 1987. Degradation of myofibrils from Rabbit, Chicken and Beef by Cathepsin L and Lysosomal Lysates. Meat Science. 21: 81-97.
Moreau, T., Gutman, N., Faucher, D. and Gauthier, F. 1989. Limited proteolysis of T-kininogen. J. Biol. Chem. 264: 4298-4303.
Morrissey, M. T., Wu, J. W., Lin, D. and An, H. 1993. Protease inhibitor effects on torsion measurements and autolysis of Pacific whitiing surimi. J. Food Sci. 58(5): 1050-1054.
Muller-Esterl, W., Fritz, H., Kellermann, J., Lottspeich, F., Machleidt, W. and Turk, V. 1985. Genealogy of mammalian cysteine proteinases inhibitors. Common evolutionary origin of stefins, cystatins and kininogens. FEBS Lett. 191: 221-226.
Mullins, D. E. and Rohrlich, S. T. 1983. The role of proteinase in cellular invasiveness. Biochim. Biophys. Acta 695: 177-214.
Murachi, T. 1983a. Calpain and calpastatin.Trends Biochem. Sci. 8: 167-169.
Murachi, T. 1983b. Intacellular Ca protease and its inhibitor protein: calpain and calpastatin. In Calcium and Cell Function Ed. Cheung, W. Y. Acaemic Press. Vol. IV : 377-410.
Murachi, T., Hatanaka, M., Yasumoto, Y., Nakayama, N. and Tanaka, K. 1981b. A quantitative distribution study on calpain and calpastatin in rat tissues and cells. Biochem. Int. 2: 651-656.
Murachi, T., Tanaka, K., Hatanaka, M. and Murakami, T. 1981a. Intracellular Ca-dependent protease (calpain ) and its high molecular weight endogenous inhibitor (calpastatin). Adv. Enzyme Regul. 19: 407-424.
Murakami, T., Hatanaka, M. and Murachi, T. 1981. The cytosol of human erythrocytes contains a highly Ca-sensitive thiol protease (calpain I) and its specific inhibitor protein (calpastatin). J. Biochem. 90: 1809-1816.
Nawa, H., Kitamura, N., Hirose, T., Asai, M., Inayama, S. and Nakanishi, S. 1983. Primary structure of bovine liver low molecular weight kininogen precursors and their two mRNAs. Proc. Natl. Acad. Sci. USA 80: 90-94.
Neurath, H. 1984. Evolution of proteolytic enzymes. Science 224: 350-357.
Neurath, H. 1989. Proteolytic processing and physiological regulation. Trend. Biochem. Sci. 14: 268-271.
Nicklin, M. J., and Barrett, A. J. 1984. Inhibition of cysteine proteinases and dipeptidyl peptidase I by egg-white cystatin. Biochem. J. 223, 245-253.
Nishiura, I., Tanaka, K., Yamato, S. and Murachi, T. 1978. The occurrence of an inhibitor of Ca2+ dependent neutral protease in rabit liver. J. Biochem. 84: 1657-1659.
Nomura, A., Itoh, Y., Nishikawa, S. and Obatake, A. 1994. The gel strengthening effect of two-step heating on the meat pastes from different fish in modori-inducing conditions. Nippon Suisan Gakkaishi 60: 667.
Nowsad, A. AKM., Kanoh, S. and Niwa, E. 1994a. Setting of surimi paste in which transglutaminase is inactivated by p-chloromercuri-benzoate. Fisheries Sci. 60: 185-188.
Nowsad, A. AKM., Kanoh, S. and Niwa, E. 1994b. Setting of surimi paste in which transglutaminase is inactivated by N-ethylmaleimide. Fisheries Sci. 60: 189-192.
Okada, Y., Teno, N., Itoh, N. and Okamoto, H. 1985. Significant effects of synthetic Gln-Val-Val-Ala-Gly and their derivatives, common sequences of thiol proteinase inhibitors, on thiol proteinase. Chem. Pharm. Bull. 33: 5149-5152.
Okitani, A., Matsukura, U., Kato, H. and Fujimaki, M. 1980. Purification and some properties of a myofibrillar protein - degrading protease, cathepsin L, from rabbit skeletal muscle. J. Biochem. 87: 1133-1143.
Pagano, M. and Engler, R. 1982. Inhibition of human liver cathepsin L by á-thiol proteinase inhibitor. FEBS Letter. 138: 307-310.
Pike, R. N. and Dennison, C. 1989. A high yield method for isolation of sheep's liver cathepsin L. Prep. Biochem. 19: 231-245.
Pike, R. N., Coetzer, T. H. T. and Dennison, C. 1992. Proteolytic active complexes of cathepsin L and a cysteine proteinase inhibitor; Purification and demonstration of their formation in vitro. Archives Biochem. Biophys. 294: 623-629.
Price, N. C. and Stevens, L. 1989. Enzymes in cell. In “Fundamentals of Enzymoloty”. Price, N. C., Stevens, L. Eds., Oxford University Press, New York. 365-422.
Rasmussen, H. and Goodman, D. B. P. 1977. Relationships between calcium and cyclic nucleoties in cell activation. Physiol. Rev. 57: 421-509.
Rich, D. H., Brown, M. A. and Barrett, A. J. 1986. Purification of cathepsin B by a new form of affinity chromatography. Biochem. J. 235: 731-734.
Rodis, P. and Hoff, J. E. 1984. Naturally occurring protein crystals in the potato. Inhibitor of papain, Chymopapain, and ficin. Plant Physiol. 74: 907-911.
Rowan, A. D., Brzin, J., Buttle, D. J. and Barrett, A. J. 1990. Inhibition of cysteine proteinases by a protein inhibitor from potato. FEBS Lett. 269: 328-330.
Rozhin, J., Wade, R., Honn, K. V. and Slonane, B. F. 1989. Membrane-associated cathepsin L: A role in metastasis of melanomas. Biochem. Biophys. Res. Commun. 164: 556-561.
Saeki, H., Iseya, Z., Sugiura, S. and Seki, N. 1995. Gel forming characteristics of frozen surimi from chum salmon in the presence of protease inhibitors. J. Food Sci. 60(5): 917-921, 928.
Sakon, M., Kambayashi, J., Ohno, H. and Kosaki, G. 1981. Two forms of Ca-activated neutral protease in platelets. Thrimb. Res. 24: 207-214.
Salvesen, G., Parkes, C., Abrahamson, M., Grubb, A. and Barrett, A. J. 1986. Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases. Biochem. J. 234: 429-434.
Sambrook, J. and Russell, D. W. 2001. In Molecular cloning, a laboratory manual, 3rd edn., vol. 3, Chapter 15: Expression of cloned genes in Escherichia coli using the bacteriophage T7 promoter. Page: 15-21. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
Sato, N., Horiuchi, T., Hamno, M., Sekine, H., Chiba, S., Yamamoto, H., Yoshioka, T., Kimura, I. And Satake, M. 1996. Kojistatin A, a new cysteine protease inhibitor produced by Aspergillus oryzae. Biosci. Biotech. Biochem. 60 (10): 1747-1748.
Sato, N., Ishidoh, K., Uchiyama, Y. and Kominami, E. 1990. Molecular cloning and sequencing of cDNA for rat cystatin b. Nucleic Acids Res. 18: 6698.
Sato, N., Ishidoh, K., Uchiyama, Y. and Kominami, E. 1992. Structure organization of the gene encoding rat cystatin b. Gene 114: 257-260.
Schwartz, W. and Barrett, A. J. 1980. Human cathepsin H. Biochem. J. 191: 487-497.
Schwartz, W. N. and Bird, J. W. C. 1977. Degradation of myofibrillar proteins by cathepsins B and D. Biochem. J. 167: 811-820.
Sherekar, S. V., Gore, M. S. and Ninjoor, V. 1988. Purification and characterization of cathepsin B from the skeletal muscle of fresh water fish, Tilapia mossambica. J. Food Sci. 53: 1018-1023.
Sloane, B. F., Rozhin, J., Robinson, D., and Honn, K. V. 1990. Role for cathepsin B and cystatins in tumor growth and progression. Biol. Chem. Hoppe-Seyler 371Suppl: 193-198.
Sotiropouplou, G., Anisowicz, A. and Sager, R. 1997. Identification, cloning, and characterization of cystatin M., a novel cysteine proteinase inhibitor, down-regulated in breast cancer. J Biol. Chem. 272: 903-910.
Suzuki, K., Tsuji, S. and Ishiura, S. 1981a. Autolysis of calcium-activated neutral protease of chicken skeletal muscle. FEBS Lett. 136: 119-122.
Suzuki, K., Tsuji, S., Kubota, S., Kimura, Y. and Imahori, K. 1981b. Limited autolysis of Ca2+-activated neutral proteas (CANP) change its sensitivity to Ca ions. J. Biochem. 90: 275-278.
Takahashi, H., Cease, K. B. and Berzofsky, J. A. 1989. Identification of proteases that process distinct epitopes on the same protein. J. Immunol. 142: 2221-2229.
Takahashi, M., Tezuka, T. and Katunama, N. 1994. Inhibition of growth and cysteine proteinase activity of Staphylococcus aureus V8 by phosphorylated cystatin αin skin cornified envelope. FEBS Lett. 355: 275-278.
Takio, K., Kominami, E., Bando, Y., Katunuma, N., and Titani, K. 1984. Amino acid sequence of rat epidermal thiol proteinase inhibitor. Biochem. Biophys. Res. Commun. 121: 149-154.
Tanaka, K., Harioka, T. and Murachi, T. 1980. Variation and multi-form of rat liver calpain and calpastatin during growth of the animal. Seikagaku. 52: 614. (Abstr. In Japanese).
Thornberry, N. A., Bull, H. G., Calaycay, J. R., Chapman, K. T., Howard, A. D., Kostura, M. J., Miller, D. K., Molineaux, S. M., Weidner, J. R., Aunins, J., Elliston, K. O., Ayala, J. M., Casano, F J., Chin, J., Ding, G. J.F., Egger, L. A., Gaffney, E. P., Limjuco, G., Palyha, O. C., Raju, S. M., Rolando, A. M., Salley, J. P., Yamin, T. T., Lee, T. D., Shively, J. E., MacCross, M., Mumford, R. A., Schmidt, J. A. and Tocci, M. J. 1992. A novel heterodimeric cysteine protease is required for interleukin-1b processing in monocytes. Nature 356: 768-774.
Towatari, T. and Katunuma, N. 1983. Selective cleavage of peptide bonds by Cathepsins L and B from rat liver. J. Biochem. 93(4):1119-1128.
Towatari, T., Tanaka, K., Yoshikawa, D. and Katunuma, N. 1978. Purification and properties of a new cathepsin from rat liver. J. Biochem. 84: 659-671.
Toyohara, H., Makinodan, Y. and Ikeda, S. 1985a. Detection of calpain and calpastatin in carp eggs. Bull. Japan. Soc. Sci. Fish. 51: 1281-1286.
Toyohara, H., Makinodan, Y. and Ikeda, S. 1985b. Detection and some properties of calpain II (high-Ca2+-requiring form of calpain) in carp (Cyprinus carpio) erythrocytes. Comp. Biochem. Physiol 81B: 583-586.
Tsushima, H. 1993. Isolation of cysteine proteinase inhibitor, cystatin A, from human nails. Arch. Dermatol. Res. 285: 418-422.
Tsushima, H., Mine, H., Hoshika, K., Kawakami, Y., Hyodoh, F., and Ueki, A. 1992. Candida albicans produces a cystatin-type cysteine proteinase inhibitor. J. Bacteriol. 174: 4807-4810.
Turk, B., Dolenc, I., Turk, V. and Bieth, J. G. 1993. Kinetics of the pH-induced inactivation of human cathepsin L. Biochemistry 32: 375-380.
Turk, V. and Bode, W. 1991. The cystatins: protein inhibitors of cysteine proteinases. FEBS Lett. 285(2): 213-219.
Van Noort, J. M. and Van der Drift, A. C. M. 1989. The selectivity of cathepsin D suggests and involvement of the enzyme in the generation of T-cell epitopes. J. Biol. Chem. 264: 14159-14164.
Walsh, T. A. and Strickland, J. A. 1993. Proteolysis of the 85-Kilodalton crystalline cysteine proteinase inhibitor from potato releases functional cystatin domains. Plant Physiol. 103: 1227-1234.
Wasson, D.; Babbitt, J. K.; French, J. S. 1992b. Characterization of a heat stable protease from arrowtooth flounder; Atheresthes stomias. J. Aquat. Food Prod. Technol. 1(3/4): 167-182.
Waxman, L. and Kerbs, E. G. 1978. Identification of two protease inhibitors from bovine cardic muscle. J. Biol. Chem. 253: 5888-5891.
Wiederanders, B., Bromme, D., Kirschke, H., Figura, K. V., Schmidt, B. and Peters, C. 1992. Phylogenetic conservation of cysteine proteinases, cloning and expression of a cDNA coding for human cathepsin S. J. Biol. Chem. 267: 13708-13713.
Yagel, S., Warner, A. H., Nellans, H. N., Lala, P. K., Waghorne, C. and Denhardt, D. T. 1989. Suppression by cathepsin L inhibitors of the invasion of amnion membranes by murine cancer cells. Cancer Res. 49: 3553-3557.
Yamashita, M. and Konagaya, S. 1990a. High activities of cathepsins B,D,H and L in the muscle of chum salmon in spawning migration. Comp. Biochem. Physiol. 95B: 149-152.
Yamashita, M. and Konagaya, S. 1990b. Partipation of Cathepsin L into extensive softening of the Muscle of Chum Salmon caught during spawning Migration. Nippon Suisan Gakkaishi. 56(8): 1271-1277.
Yamashita, M. and Konagaya, S. 1990c. Purification and characterization of cathepsin L from the white muscle of chum salmon, Oncrohynchus Keta. Comp, Biochem,Physiol. 96B: 733-737.
Yamashita, M. and Konagaya, S. 1991. Hydrolytic action of Salmon Cathepsins B and L to muscle structural proteins in respect of muscle softening. Nippon Suisan Gakkaishi. 57(10): 1917-1922.
Yamashita, M., Henmi, H., Ueda, T., Obara, M., Taro, T., Nishioka, F. and Konagaya, S. 1996. Marked proteolysis occurring during thermal gel formation of the mined meat from matured chum salmon and restraining effect of protease inhibitor on gel-degradation. Nippon Suisan Gakkaishi. 62(6): 934-938.
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