請用此 Handle URI 來引用此文件：
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/76072完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.author | Ching-Hsiang Hung | en |
| dc.contributor.author | 洪靜香 | zh_TW |
| dc.date.accessioned | 2021-07-01T08:17:47Z | - |
| dc.date.available | 2021-07-01T08:17:47Z | - |
| dc.date.issued | 1994 | |
| dc.identifier.citation | Adam. A., Petit. J-F., Lefrancier. P. and Lederer. E. 1981 Muramvl peptides. Mol. and Cell. Biochem. 41:27-47
Azuma. I. 1992 Development of the cytokine inducer romurtide: experimental studies and clinical application, Trends Pharmcol. Sci. 13:425-428 Barr. P. J. 1992 Mammalian subtilisins: the long-sought dibasic processing endoprotease. Cell 66:1-3 Bayne. C. J. 1986 Pronephric Leucocytes of Cyprinus carpio: Isolation, separation and characterization, 1’eterinary Immunol. Immunopathol. 12:131-151 Beaumont. A., Bathe, B., Le Moual Herve’, Boileau, G., Crine, P., Ffournie’-Zaluski, M-C., Roques, B. P. 1992 Charge polarity reversal inverses thespecificity of neurtral endopeptidase-24. 11. J. Biol. Chem. 267:2148-2141 Bernt, E., Bergmeyer, H. U. 1974 Colorimetric assay with L-lacate, NAD phenazine Methosulphate and INT. In methods of enzymatic analysis, ed. Bergmeyer, H. U. pp579-58l, Academic Press, Orlando Bond J. S., Butler. P. E. 1987 Intracellular proteases. Annu. Rev. Biochem. 56-333-64 Bradford, M. M. 1976 A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254 Bryan, P., Pantoliano, M. W., Quill, S. G., Hsiao, H-Y., Poulos, T. 1986 Site-directed mutagenesis and the role of the oxyanion hole in subtilisin. Proc. Natl. Acad. Sci. USA 83:3743-3745 Busiek, D. F., Ross, F. P., McDonnell, S. Murphy, G. Matrisian, L. M. and Welgus, H. G. 1992 The matrix metalloprotease matrilysin (pump) is expressed in developing human mononuclear phagocytes, J. Blot. Chem. 267:9087-9092 Butler, P. E., McKay M. J. and Bond, J. S. 1987 Characterization of meprin, a membrane-bound metalloendopeptidase from mouse kidney, Bichem. J. 241:229-235 Byron. J. W. 1972 Evidence for a beta adrenergic receptor initiating DNA synthesis in haemopoietic stem cells. Exp. Cell. Res. 71:228-32 Carruth, L. M.. Demczuk. S. and Mizel. S. B. 1991 Involvement of a calpain-like protease in the processing of the murine interleukin- la precursor, J. Biol. Chem. 266:12162-12167 Chen, W-T. 1992 Membrane proteases: roles in tissue remodeling and tumor invasion, Curr. Opin. Cell Biol. 4:802-809 Corey, D. R. Craik. C. S. 1992 An investigation into the minimum requirements for peptide hdrolysis by mutation of the catalytic triad of trypsin. J. Am Chem. Soc. 114:1784-1790 Dahmann. B., Rutschmann, M., Kuehn. L.. Reinauer, H. 1985 Activation of the multicatalytic proteinase from rat skeletal muscle fatty acids or sodium dodecvl sulphate, Biochem. J. 228:171-177 Danscher. D. 1982 Exogenous selenium in the brain: a histochemical technique for light and electron microscopical localization of catalytic selenium bonds, Histochem. 76:281-293 DeMartino, G. N., Blumenthal, D. K. 1982 Identification and partial purification of a factor that stimulates calcium-dependent proteases, Biochemistry 21:4297-4303 Dowdle. E. B., Heussen C, 1980 Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Anal. Biochem. 102:196-202 Dunn. B. M. 1990 Determination of protease mechanism. In Preoteolytic enzymes. ed. Beynon, R J.. Bond. J. S. pp.57-82. IRL Press, Oxford Felten, S. Y., Olschowka, J. A. 1987 Noradrenergic sympathetic innervation of the spleen: Ⅱ. Tyrosine hydroxy1ase (TH)-positive nerve terminals form synaptic-like contacts on lymphocytes in the splenic white pulp. .J. Neurosci. Res. 18:37-48 Fletterick, R. J., Phillips. M. A. 1992 Proteases. Curr. Opin. Struct. Biol. 2:713-720 Ghidyal. N.. McNeil. H.P.. Stechschulte. S.. Austen. K. F.. Silberstein. D.. Gurish. M. F. Somerville. L. L.. 1992 IL-10 induces transcription of the gene for mouse mast cell protease-1. a serine protease preferentially expressed in mucosal mast cells of Trichinella spiralis-infected mice. J. Immunol. 149:2123-2129 Ghildyal. N., McNeil. H.P.. Gurish. M. F.. Austen. K. F.. Stevens. R L. 1992 Transcriptional reguation of the mucosal mast cell-specifice protease gene. MMCP-2. by interleukin 10 and interleukin-3. J. Biol. Chem. 267:8473-8477 Goldstein. S. M.. Leong. J.. Bunnett. N. W. 1991 Human mast cell proteases hydrolyze neurotensin. kinetensin an Leu5-enkephalin, Peptides 12:995-1000 Guasch. A., Call, M., Aviles. F. X., Huber. R. 1992 Three-dimensional structure of porcine pancreatic procarboxypeptidase A: a comparison of the A and B zymogens and their determinants for inhibition and activation. J. Mol. Biol. 224:141-157 Gurish. M. F., Ghildyal. N., McNeil, H.P., Austen, K. F., Gillis. S., Stevens, R. L., 1992 Differential expression of secretory granule proteases in mouse mast cells exposed to IL-3 and c-kit ligand, J. Exp. Med.175:1003-1012 Haass. C., Selkoe, D. J. 1993 Cellular processing of beta amyloid precursor protein and the genesis of amyloid beta-peptide. Cell 75:1039-1042 Harlow, E., Lane. D., 1988a Antibodies: a laboratory manual, pp53-l38, Cold Spring Harbor Laboratory Press. NY Harlow. E., Lane. D., 1988b Antibodies: a laboratory manual, pp471-5 10, Cold Spring Harbor Laboratory Press, NY Hayes. M.P., Berrebi, G. A. Henkart, P. A. 1989 Induction of target cell DNA release by the cytotoxic T lymphocyte granule protease granzyme, J. Exp. Med 170:933-946 Hedstrom, L., Szilagyi, L., Rutter, W. J., 1992 Converting trypsin to chymotrypsin the role of surface loops. Science 255:1249-1253 Ho, W-H. 1993 Purification of a multifunctional protein kinase inhibitor from carp headkidney. In master thesis of Graduate Institute of Biochemical Sciences, National Taiwan University Hollecker, M. 1989 Protein structure, ed. Creighton, T. E., ppl45-l53, IRL Press, UK Hsu Y-C. 1991 Purification and characterization of a catecholamines-releasing factor from carp. In master thesis of Graduate Institute of Biochemical Sciences, National Taiwan University Jenne. D. E., Tschopp. J. 1988 Granzymes: a family of serine proteases in granules of cytolytic T lymphocytes, Curr. Top. Microbiol. Immunol. 140:33-47 Jones, I. C., Mosley, W. 1980 General comparative and clinical endocrinology of the adrenal cortex, ed. Jones, I. C. and HEnderson, I. W., pp428. Academic Press, Orlando Kerr, L. D., Miller, D. B., Matrisian, L. M. 1990 TGF-beta1 inhibition of transin/stromelysin gene expression is mediated through a fos binding sequence. Cell 61:267-278 Khouri, H. E., Vernet, T., Menard, P., Parlati, F., Laflame, P., Tessier, D. C., Gour-Salin, B., Thomas. D. Y., Storer, A. C. 1991 Engineering of papain: selective alteration of substrate specificity by site-directed mutagenesis, Biochemistry 30:8929-8936 Kinoshita, A., Urata, H., Bumpus, F. M., Husain. A. 1991 Multiple determinants for the high substrate Specificity of an angiotensin Ⅱ-foring chymase from the human heart. J. Biol Chem. 266:19192-19197 Kleiner D. E. Jr. and Stetler-Stevenson. W. G. 1993 Structural biochemistry and activation of matrix metalloproteases, Curr. Opin. Cell Biol. 5:891-897 Laboratory Press. NY Levine, J. E., Ramirez, V. D., 1986 Measurement of Neuropeptide release. In Methods Enzvmol. 124:466-494. Academic Press. Orlando Lowe. C. R., Pearson. J. C. 1984 Affinity chromatography on immobilized dyes. in Methods Emzpnol,104: 97-113. Academic Press. Orlando Mellman. I., Fuchs. R., Helenius. A. 1986 Acidification of the endocytic and exocytic pathways. Anntt. Rev. Biochem. 55:663-700 Merrill. C. R., Goldman. D., van Keuren. M. L. 1984 in Methods Enzymol. Ed. Jakoby. W. B., 104:441-447, Academic Press. Orlando Mignatti. P. and Rifkin. D. B. 1993 Biology and biochemistry of proteinases in tumor invasion. Physiol. Rev., 73(1):161-195 Miura, M., Zhu. H., Rottello, R., Hartwieg, E. A., Yuan, J. 1993 Induction of apoptosis in fibroblasts by IL-beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3, Cell 75:653-660 Muphy, G., Allan, J. A., and Willenbrock, F., Cockett. M. I., O’Connell, J. P. and Dochertv, A. J. 1992 The role of the c-terminal domain in collagenase and stromelysin specificity. J. Biol. Chem. 267:9612-9618 Nagase, H., Barrett. A. J. and Woessner, J. R 1989 Nomenclature and glossary of the matrix Metalloproteinase, In matrix metalloproteinase and inhibitors. Proceedings of the matrix metalloproteinase conference. S, estin Beach, Florida, september 11-15 Neurath, H. 1990 The diversity of proteolytic enzymes, In proteolytic enzymes. Ed. Beynon, R J., Bond, J. S. pp. 1-14, IRL Press, Oxford Nomura. K., Tanaka, H. Kikkawa, Y., Yamaguchi, M. and Suzuki, N. 1991 The specificity of sea urchin hatching enzyme (envelysin) places it in the mammalian matrix metalloproteinase family, Biochemistry 30:6115-6123 Pearl. L. H. 1987 The catalytic mechanism of aspartic proteinases, FEBS Letters 214(1):8-12 Philips. M. A.. Kaplan, A. P., Rutter, W. J., Bartlett, P. A. 1992 Transition-state Characterization: a new approach combinging inhibitor analogues and variation in enzyme structure, Biochemistry 31:959-963 Qian. Z., Gilbert, M. E., Colicos, M. A., Kandel, E. R, Kuhl, D. 1993 Tissue-plasminogen activator is induced as an immediate-early gene during seizure, kinding and long-term potentiation, Nature 361:453-457 Ray. C. A., Black R. A. Kronheim, S. R., Greenstreet, T. A., Sleath. P. R., Salvesen. G. S. Pickup. D. J. 1992 Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1b converting enzyme Cell 69:597-604 Reynolds D. S., Stevens, R L., Lane, W. S., Carr, M. H., Austen, K. F., Serafin, w. E. 1990 Different mouse mast cell populations express various combinations of at least six distinct mast cell serine proteases, Proc. Natl. Acad. Sci. USA 87:11174-11178 Reynolds D. S., Gurley, D. S., Austen, K. F. 1992 Cloning and characterization of the novel gene for mast cell carboxypeptidase .A, J. Clin. Invest. 89:273-282 Rydel. T. J., Tulinsky, A., Bode, W., Huber, P.. 1992 Refinde structure of the hirudin-thrombin complex. J. Mol. Biol. 221:583-601 Schagger, H., Jagow, G. V., 1987 Tricine-sodium dodecyl sulfate-polyacrylamine gel electropphoresis for the Separation of protein in the range from Ito 100 kDa, Anal. Biochem. 166:368-379 Schechter, I., Berger. A. 1967 On the size of the active site in proteases, Biochem. Biophys. Res. Commun. 27(2) l57,.l62 Schwartz, L. B. 1994 Mast cells: functin and contents, Curr. Opin. Immunol. 6:91-97 Scopes, P., K. 1987 Dye-ligands and multifunctional absorbents: an empirical approach to affinity chromatography. Anal. Bioem. 165:235-246 Sedgwick, J. B. Calhoun.’ J., Gleich, G. J., Kita, H., Abrams, J. S., Schwartz, L. B., Volovitz, EB.. Ben-Yaakov, M., Busse. W. 1991 Immediate and late airway response of allergic rhinitis patitienmts to segmental antigen chal1en characterization of eosinophil and mast cell mediators. Am. Rev. Resppiar. Dis.143:563-568 Shi, I., Kraut, R. P., Aeberld, R., Greenberg, A. H. 1992 A natural killer cell granule protein that: intrduces DNA fragmentation and aptosis. J. Exp. Med. 175:553-566 Ship, M. A., Vijayaraghay, J., Schmidt, E. V., Masteller, E. L., D’Adamio, L., Hersh, L. B., Reimnhaerz, E.L., 1989 Common acute mphoblastic leukemia antigen (ALLA) is active neutral endopepidase 24.11(‘enkephalinase’): directedence by cDNA transfection analysis. Proc. Natl. Acad. Sci. USA 86:2977-30l Simmons. W. H. and Oraki. A. T. 1992 Membrane-bound aminopeptidase P from bovine hung.;. J. Biol. Chem. 267(7):4897-4903 Singh. U., Millson, S.. Sth P. A... . Owen. J. J. T. 1979a Identificaiton of beta adrenorecptorsrs during thymocyte ontogeny in mic Eur. J. Immunol. 9:31-35 Singh, U. 1979b Effect (catecholamines on lymphopoiesis in fetal mouse thymic explants.,: Eur. J. Immunol. 14:757-59 Sisodia. S. S. 1992 beta-ayloid precusor protein cleavage by a membrane -bound protease. Prcoc. Natl. Acad. Sci. USA 89:6075-619 Springman, F. B., Anglet, E. L., Birkedal-Hansen, H. and van Wart, H. E. 1990 Multiple mmoodes of activation of latent human broblast collagenase - evidence for the role of a cys73 active-site zinc C cormplex in latency and a cysteine Such mechanism for activation, Proc. Natl. Acad. Sci. USA 87:364-368 Suttles, J. Gin, J. G., and Mzel, S. B. 1990 IL-I secretion by macrophages, J. Immunol. 144:175-1822 Thornberry, N. A., Bull, HG., Calaycay, J. R., Chapman, K. T., Howard, A. D., Kostura, M. I., MMillller, D. K., Molineaux, S. M., Wedner, J. R., Aunins, J. et al 1992 A novel heterodimeric cysteine prcotease is required for interleulcin-1b rocessing in monocytes, Nature 356:768-774 Turner, A. J. 1987 Endoeptidase-24.11 and neuropeptide metabolism, in Neuropeptides and their Peptidases ed. Turner, A , ppl81-201, Chichester: Ellis Horwood Ltd Woessner. F. J. jr. 1991fatrix metalloproteinase and their inhibitors in connective tissue remmowdeling, FASEB J. 5:2145-21154 Yamaguchi, T., Kido, H., ukase, M., Fujita, T. and Katunuma, N. 1991 A membrane-boand metallo-endopeptidase from rat kidey hydro1yzing parathyroid hormone: purification and characterization, Eur. J. Biochem. 200:563-571 Yamaguchi, T., Kido, H. nd Katunuma, N. 1992 A membrane-bound metallo-endopeptidse from rat kidney. Eur. J. Biochem. 24:547-552 Zapata. A. 1979 Ultrastructral study of the teleost fish kidney, Dev. Comp. Immunol. 3:55-65 Zhou, H., Bernhard, E. J., Fox, F. E. and Billings, P. C. 1993 Induction of metalloproteinase activity in human T-lymphocytes, Biohem Biophys. Acta 1177:174-178 Zunno, S. J., Bleackley, R. C., Martinez, J., Hudig, D. 1990 RNKP-1, a novel natural kiler-asssonciated serine protease gene: clonedrom PNK-16 cytotoxic lymphocytes. J. Immunol. 144:2001-2009 上野洋一郎，陳秀男，郭光雄 編 1989魚類之正常及病理組織學 P133-136 國立臺灣大學漁業推廣委員會出版 | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/76072 | - |
| dc.description.abstract | 目前吾已從鯉魚的頭腎(lleadkidney)中純化得到一個25kDa的蛋白質水解酵素；純化的方法是將頭腎研磨均質後取上清液，先通過Dye Reactive Blue 72 agarose affinity液狀層析管柱，經過透析濃縮後，再利用FPLC Mono-P液狀層析管柱分析。從銀染色蛋白質電泳膠片圖的結果顯示其分子量與純度。分析各類蛋白質水解酵素的抑制劑對此25kDa蛋白質水解酵素的抑制能力，發現金屬螫合劑的抑制效果最佳，因此推論它是一個耦合金屬蛋白質水解酵素，命名為MP-25。從染鋅離子分佈的頭腎切片結果中，知道頭腎富含鋅離子，也許可佐證上述事實。在勝?水解實驗中，以substance P和各胺基酸長度的Bradykinin為MP-25的基質，被水解的勝?片斷經HPLC的純化，再由氨端胺基酸序列分析得知，MP-25喜切厭水性胺基酸的位置，例如phenylalanine；另一特色是基質勝?長度要七個以上。接者，以此MP-25為抗原打入天竺鼠中引發對抗MP-25的專一性抗體。再利用西方點墨法分析此MP-25的分佈，結果顯示它存在於頭腎、脾臟和腎臟中。因為鯉魚的器官分化程度與高等哺乳動物不同，前述的那三種器官都兼有免疫功能。而在灌流實驗中，以化學物質刺激頭腎活體組織，分析刺激前後釋放蛋白質種類和數量的變化。經由酵素分佈電泳圖和西方點墨法的結果得之，MP-25以高濃度的鉀離子(50mM)、romutide、腎上腺素刺激下，會自頭腎組織中釋放。從上述結果可知釋放MP-25是刺激免疫組織的效應之一，推論在鯉魚體的免疫系統中MP-25可能扮演某種角色。 | zh_TW |
| dc.description.abstract | We have purified a 25kDa protease from the headkidney of carp by sequential column chromatography on Dye Reactive Blue 72 affinity column and FPLC Mono-P column. Using various inhibitors specific for different classes of proteases, we found metal chelators had better inhibitory effects on the activity of the 25kDa protease. Therefore, we have identified this 25kDa protease as a member of metalloprotease (MP-25). The strong staining of headkidney sections by a histochemical method using sodium selenite and silver has indicated that carp headkidney is rich in zinc ion. Furthermore, we have determined the substrate specificity of this protease by sequence analysis of the digested peptide fragments from Lys-bradykinin and substance P. MP-25 prefers cutting P1 site at hydrophobic amino acid residues, e.g. Phe-Ser and Gly-Phe in Lys- bradykinin, and Gln-Phe and Phe-Phe in substance P. We have also raised a polyclonal antiserum against MP-25 and found that MP-25 is present in the headkidney, kidney and spleen, all of which are responsible for immune functions in the carp. In addition, we have demonstrated that a high concentration of potassium, romutide or epinephrine stimulated the secretion of MP-25 from perfused headkidney. From these results, it is very likely that MP-25 is secreted from the headkidney in response to stimulation of immune system. Therefore, MP-25 may mediate certain functions of fish immune system. | en |
| dc.description.provenance | Made available in DSpace on 2021-07-01T08:17:47Z (GMT). No. of bitstreams: 0 Previous issue date: 1994 | en |
| dc.description.tableofcontents | 致謝. . . . . . . . . . . . . . . . . . 2 中文摘要. . . . . . . . . . . . . . . . . . . . 3 英文摘要. . . . . . . . . . . . . . . . . . . . . 4 目錄. . . . . . . . . . . . . . . . . . . . . . . . . . . 5 壹、緒論. . . . . . . . . . . . . . . . . . 8 一、蛋白質水解酵素的重要性及研究. . . . . . . . . . . . . . 8 二、蛋白質水解酵素的分類. . . . . . . . . . . . . . . . . 8 三、蛋白質水解酵素的催化機制簡介. . . . . . . . . . . . . . . . 9 1. Serine proteases: . . . . . . . . . . . . . . . . . . . . . . . . . . . . 9 2. Cysteine proteases: . . . . . . . . . . . . . . . . . . . . . . . . . . . 9 3. Aspartic proteases: . . . . . . . . . . . . . . . . . . . 10 4．Metalloproteases: . . . . . . . . . . . . . . . . . . . . . . . 10 四、蛋白質水解酵素的基質專一性. . . . . . . . . . . . . . . . . . . . 10 五、蛋白質水解酵素的調節. . . . . . . . . . . . . . . . . . . . . . . 11 1．細胞的隔間(compartmentalization): . . . . . . . . . . . . . 11 2．調節蛋白質水解酵素活性之蛋白質： . . . . . . . . . . . . . 11 3．新陳代謝中間物(metabolites): . . . . . . . . . . . . . . 12 4．基因調節： . . . . . . . . . . . . . . . . . . 12 六、鯉魚頭腎 . . . . . . . . . . . . . . . . . . . . . . . .12 1．結構與發生：. . . . . . . . . . . . . . . . . . . . . . . . . 12 2．內分泌功能： . . . . . . . . . . . . . . . . . . . . . . 12 3．免疫功能： . . . . . . . . . . . . . . . . . . . . . . . . 13 七、與免疫功能有關的蛋白質水解酵素. . . . . . . . . . . . . . . . 13 1．肥大細胞(mast cells)內的neutral proteases: . . . . . 13 2．活化cytokines: . . . . . . . . . . 11 3. Cranzymes： • • • • • • 14 ' 貳、實驗材料與方法 . . . . . . . 16 一、實驗藥品. . . . . . . 16 二、實驗動物• • • • • • • 16 三、主要儀器 • • • • • • • • 16 四、實驗方法• • • • • • 17 1．鯉魚頭腎蛋白質水解酵素的純化：• • • • • • 17 2. SDS聚丙醯膠胺電泳分析(SDS-PAGE): … … 18 3．蛋由質定量方法：. . . . . . . . . . . . . . . . . . 21 4．蛋白質分子質量估算. . . . . . . . . . . . . . . . . . 21 5．蛋白質水解酵素活性分析：. . . . . . . . . . . . . . . . . . 21 6．蛋白質水解酵素基質選擇性分析：. . . . . . . . . . . . . . . . . . 24 7．蛋白質水解酵素抗體血清的製備：. . . . . . . . . . . . . . . . . . 24 8．西方點墨分析法(Western blotting) . . . . . . . . . . . . . . . . . . 25 9．各種組織萃取液的製備： . . . . . . . . . . . . . 26 10. 免疫組織化學分析： . . . . . . . . . . . . . . . . . . . . . 27 11．組織灌流法： . . . . . . . . . . . . . . . . . . . . . . . . . . 29 12．鋅離子染色： . . . . . . . . . . . . . . . . . . . . . . . . . . . . 32 參、結果. . . . . . . . . . . . . . . . .34 一、MP-25的純化• • • • • • •34 1．鯉魚各器官內蛋白質水解酵素的分佈調查： . . . . . . . 34 2. Dye Reactive Blue 72 agarose affintiy column: . . . . . . . . . . 34 3. FPLC Mono-P chromatofocusing: . . . . . . . 34 4．建立純化表：. . . . . . . . . . . . . . . . . .35 二、 MP-25的專一性與生化特性. . . . . . . . . . . . . 35 1．鑑定蛋白質水解酵素的種類： . . . . . . . . . . . . . . . . . .35 2．鑑定MP-25的基質專一性. . . . . . . . . . . . . . . . . .35 三、MP-25的組織分佈. . . . . . . . . . . . . . . . . . 36 1．含MP-25的器官：. . . . . . . . . . . .36 2．MP-25在頭腎中的分佈： . . . . . . . . . . .36 四、MP-25從頭腎的釋放. . . . . . . . . . . .36 五、頭腎的鋅離子染色. . . . . . . . . . . .37 肆、討論. . . . . . . . . . . .38 一、MP-25的純化. . . . . . . . . . .38 二、基質的選擇 . . . . . . . . . . . . . 39 三、耦合金屬蛋白質水解酵素的功能探討 . . . . . .39 1. plasma membrane metalloprotease：. . . . . . . . . . . .40 2．Matrix metalloprotease: . . . . . . . . . . . .40 四、MP-25從頭腎的釋放. . . . . . . . . . . .41 五、組織內鋅離子的分佈. . . . . . . . . . . .42 參考文獻. . . . . . . . . . . . . . . . . . . . . . 44 圖表說明. . . . . . . . . . . . . . . . . . . . .48 | |
| dc.language.iso | zh-TW | |
| dc.title | 鯉魚頭腎25kDa耦合金屬水解酵素之純化 | zh_TW |
| dc.title | Purification of a 25kDa Metalloprotease from Carp Headkidney | en |
| dc.date.schoolyear | 82-2 | |
| dc.description.degree | 碩士 | |
| dc.relation.page | 72 | |
| dc.rights.note | 未授權 | |
| dc.contributor.author-dept | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 生化科學研究所 | zh_TW |
| 顯示於系所單位： | 生化科學研究所 | |
文件中的檔案：
沒有與此文件相關的檔案。
系統中的文件，除了特別指名其著作權條款之外，均受到著作權保護，並且保留所有的權利。