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DC 欄位 | 值 | 語言 |
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dc.contributor.author | S. M. Jong | en |
dc.contributor.author | 鍾松穆 | zh_TW |
dc.date.accessioned | 2021-07-01T08:20:38Z | - |
dc.date.available | 2021-07-01T08:20:38Z | - |
dc.date.issued | 1980 | |
dc.identifier.citation | Abita, J., Lazdunski, M., Bonsen, P. P. M., Pieterson, W. A., deHaas, G. H H. (1972) Eur. J. Biochem. 30, 37-47. Adler, A. J., Greenfield, N. J., and Fasman, G. D. (1973) in “Methods in Enzymo1ogy”, (Hirs, C. H.W. ed.), 27D, pp 675-735. Agogbua, S. I. O., and Wynn, C. H. (1976) Biochem. J. 153, 415. Aguiar, A., deHaas, G. H., Jansen, E. H. J. M., Slotboom, A. J., and Williams, R. J. P. (1979) Eur. J. Biochem. 100, 511-518. Aleksiev, B., and Shipolini, R. (1973) Int. Sym. on Polymer Varna (Bulgaria), 1, 417. Apsalon, U. R., Gotgilf, J. M., Gritsuk, V. J., Magazanik, L. G., Miroshnikov, A. I., and Slavnova, T. I. (1979) Toxicon, 17, Supple, 1, 2. Bailey, J. L. (1967) “Techniques in Protein Chemistry”, 2nd ed. Barman, T. E. and Koshland, D. E. JR. (1967) J. Biol. Chem. 242, 5771-5776. Barth, G., Voelter, W., Bunnenberg, E., and Djerassi, C. (1972) J. Am. Chem. Soc. 94, l293-1298. Bellin, J. S., Yankus, C. A. (1968) Arch. Biochem. Biophys. 123, 18. Bennett, H. P. J., Elliott, D. F., Evans, B. E., Lowry, P. J., and McMartin, C. (1972) Biochem. J. 129, 695-701. Billmeyer, F. W. JR., Johnson, G. W., and Kolley, R. N. (1968) J. . Chromatogr. 34, 316-321, 322-331. Botes, D, P., and Viljoen, C. C. (1974) J. Biol. Chem. 249, 3827-3835. Braganca, B. M., and Khandeparker, V. G. (1966) Life Sci. 5, 1911-1920. Bredderman, P. J. (1974) Anal. Biochem. 61, 298-301. Brewer, J. M., Pesce, A. J., and Ashworth, R. B. (1974) “Experimental Te chniques in Biochemistry”, Prentice-Hall Inc. Bokerhoff, H., and Jensen, R. G. (1974) “Lipolytic Enzymes”, Academic P., New York. Brossmer, R., and Bohn, B. (1974) F. E. B. S. Lett. 42, 116. Chang, W. C., and Lo, T. B. (1975) J. Chinese Biochem. Soc. 4, 43-50. Chang, W. C., and Lo, T. B. (1976) in “Memorial Vol. to President Chiang Kai-shek”, pp 587-617, Academia Sinica, R. O. C. Chapus, C., and Semeriva, M. (1976) Biochemistry, 15, 4988. Chen, Y. H., Yang, J. T. (1971) Biochem. Biophys. Res. Commun. 44, 1285. Chiang, H. C., Chang, W. C., and. Lo, T. B. (1973) J.Chinese Biochem. Soc. 2, 16-24. Concon, J. M. (1975) Anal. Biochem. 67, 206-219. Cruickshank, W. H., and Kaplan, H. (1975) Biochem. J. 147, 411. Cuatrecasas, P., Fuchs, S., and Anfinsen, C. B. (1968) J. Biol. Chem. 243, 4787-4798. Dann, L. G., and Britton, H. G. (1974) Biochem, J. 137, 405. Davis, B. J. (1964) N. Y. Acad. Annals, 121, 404. DeHaas, G. H., Postema, N. M., Nieuwenlauizen, W., and van Deenen, L. L. M. (1968) Biochim. Biophys. Acta, 159, 103-117. DeHaas, G. H., Slotboom, A. J., Bonsen, P. P. M., vanDeenen, L. L. M., Maroux, S., Puigserver, A. and Desnuelle, P. (1970) Biochim. Biophys. Acta, 221, 31-53. Delori, P. J. (1973) Biokhimie, 55, 1030. Dennis, E. A. (1977) J. Biol. Chem. 252, 2405-2411. Dijkstra, B, W., Drenth, J., Kalk, K. H., and Vandermaelen, P. J. (l978) J. Mol. Biol. 124, 53-60. Doery, H. M., and Pearson, J. E. (1964) Biochem. J. 92, 599-602. Donovan, J.W. (1973) in “Methods in Enzymology”, Hirs, C. H. W. ed. 27D, pp 525-548. Drenth, J., Enzing, C. M., Kalk, K. H., Vessies, J. C. A. (1976) Nature, 264, 373-377. Duggleby, R. G., and Kaplan, H. (1975) Biochemistry, 14, 5168. Eaker, D. (1975) Toxicon, l3, 90-91. Edelhoch, G. (1967) Biochemistry, 6, 1948-1955. Elliott, W. B. (1978) in “Biology of the Reptilia” Vol. 8B, pp 163 (Gans, C., and Gans, R. A. eds.), London, Academic Press. Evenberg, A., Meyer, H., Gaastra, W., Verheij, H. M., and deHaas, G. H. (1977) J. Biol. Chem. 252, 1189-1196. Fernley, H. N., Bisaz, .S. (1968) Biochem. J. 107, 279. Fife, W. K. (1967) Biochem. .Biophys. Res. Commun. 28, 309. Fleer, E. A. M., Verheij, H. M., and deHaas, G. H. (1978) Eur. J. Biochem. 82, 261-269. Fletcher, J. B., Elliott, W. B., Ishay, J., and Rosenberg, P. (1979) Toxin, 17, 591-599. Fohlman, J., and Eaker, D. (1977) Toxin, 15, 385-393. Fohlman, J.., Lind, P., and Eaker, D. (1977) F. E. B. S. Lett. 84, 367. Fontana, A., Scoffone, E., and Benassi, C. A. (1968) Biochemistry, 7, 980. Furth, A. J., and Hope, D. B. (1969) Biochem. J. l16, 543-553. Fuson, R. C., Shriner, R. L., Curtin, B. Y. (1964) “Systematic Identification of Organic Compounds” . Gaitonde, M. K., and Dovey, T. (1970) Biochem. J. 117, 907-911. Goodwin, T. W., and Morton, R. A. (1946) Biochem. J. 40, 628-632. Greenfield, N. J. (1974) Biochemistry, 13, 4494. Halpert, J., and Eaker, D. (1976) J. Biol. Chem. 251, 7243-7347. Halpert, J., Eaker, D., and Karlsson, E. (1976) F. E. B. S. Lett. 61, 72-76. Heinrikson, R. L., Krueger, E. T., and Keim, P. S. (1977) J. Bio1. Chem. 252, 4913-4921. Hiramatsu, A., Tsurushin, S, and Yasunohu, K. Y. (1975) Eur. J. Biochem. 57, 587. Holzwarth, G, M., and Doty, P. (1965) J. Am. Chem. Soc. 87, 218. Howard, N. L. (1975) Toxicon, 13, 21-30. Huang, K. S., and Law, J. H. (1978) Adv. exp. Med. Biol. 101, 177-183. Hugli, T. E., and Moore, S. (1972) J. Biol. Chem. 247, 2828-2834. Jencks, W. P. (1970) in “Chemical Reactivity and Bio1ogical Role of Functional Groups in Enzymes”, Smellie, R. M. S. ed. pp 59-80. Academic Press. Joubert, F. J. (1975a) Biochim. Biophys. Acta, 379, 329-344. Joubert, F. J. (1975a’) Biochim. Biophys. Acta, 379, 345-349. Joubert, F. J. (1975b) Eur. J. Biochem. 52, 539-554. Joubert, F. J. (1977) Biochim. Biophys. Acta, 493, 216-227. Kandel, M., Gornall, A. G., Cybulsky, D. L., and Kandel, S. I. (1974) Biochem. Biphys. Res. Commun. 56, 568. Kenner, R. A., and Neurath, H. (1971) Biochemistry, 10, 551-557. Kochetkov, S. N., Bulargina, T. V., Sashchenko, L.P., and Severin, E. S. (1976) F. E. B. S. Lett. 71, 212. Kocholaty, W. (1966) Toxicon, 3, 175-186. Kocholaty, W., and Ashley B. D. (1966) Toxicon, 3, 187-194. Kondo, K., Narita, K., aria Lee, C. Y. (l978a) J. Biochem. Japan, 83, 101-115. Kondo, K.,Toda, H., and Narita, K. (l978b) J. Biochem. Japan, 84,1291-1308. Kronman, M. J., and Robbins, F. M. (1970) in “Fine Structures in Proteins and Nucleic Acids”, chapter 4. Fasman, G. D., and Timasheff, S N. eds. M. Dekker, Inc., New York. Kub n, M. (1975) J. Chromatogr 103, 1-12. Kumagai, H., Utagawa,T., and Yamada, H. (1975) J. Biol. Chem. 250, 1661. Lehninger, A. L. (1975) “Biochemistry” Lewis, R. V., Roberts, M. F., Dennis, E. A., and Allison, W. S. (1977) Biochemistry, 16, 5650-5654. Lichtenberg, D., Zilberman, Y., Greenzaid, P., and Zamir, S. (1979) Biochcmistry, 18, 3517-3525. Litvinko, N. M., Khurgin, Y. I., and Kaverzneva, E. D. (1977) Biokhimia 42, 85-94. Liu, T. Y., and Chang, Y. H. (1971) J. Biol. Chem. 246, 2842-2848. Lo, T. B., Chang, W. C., and Chang, C. S. (1972) J. Formosan Med. Assoc. 71, 318-322. Lo, T. B., Chen., Y. H., and Lee, C. Y. (1966) J. Chinese Chem. Soc. II 13, 25-37. Long, C., and Penny, I. F. (1957) Biochem. J. 65, 382-389. Loosemore, M. J., and Pratt, R. F. (1976) F. E. B. S. Lett. 72, 155-158. Lu, H. S. Lee, M. T., and Yang, H. M. (1979) personal communication. Matsibara, H., and Sasaki, R. M. (1969) Biochem. Biophys. Res. Commun. 43, 103-114. Matyr, R. J., and Benisek, W. F. (1975) J. Bio1. Chem. 250, 1218. Meienhofer, J. (1965) Nature, 205, 73. Meyer, H., Vorhoef, H., Hendriks, F. F. A. Slotboom, A. J., and deHaas, G. H. (1979) Biochemistry, 18, 3582-3588, 3589-3597. Miles, E. W. (1977) in “Methods in Enzymology”, 47, 431-442. Mohamed, A. H., Kamel, A., and Ayobe, M. H. (1968) Toxicon, 6, 293-298. Munjal, D., and Elliott, W. B. (1971) Toxicon, 9, 403. Nakanishi, K., Yamanoto, S., Matsuno, R., and Kamikubo, T. (1977) Agric. Biol. Chem. 41, 1465-1473. Omori-Satoh, J., Lang, J., Breithaupt, H., and Habermann, E. (1975) Toxicon, 13, 69-71. O’vadi, J., Libor, S., ano Elodi, P. (1967) Biochim. Biopbys. Acta, 2, 455. Patchornik, A., Lawson, W. B., and Witkops, B. (1958) J. Am. Chem. Soc, 80, 4747-4749. Pieterson, W. A., deHaas, G. H. (1972) Eur. J. Biochem. 30, 37-47. Pieterson, W. A., Volwerk, J. J., and deHaas, G. H. (1974) Biochemistry, 13, 1439-1445. Pincus, M., Thi, L. L., and Carty, R. P. (1975) Biochemistry, 14, 3653. Pons, M., Nicolas, J. C., Boussjeux, A. M., Descomps, B., and dePaulet, A. C. (1973) F. E. B. S. Lett. 31, 256. Puijk, W. C., verheij, H. M., and deHaas, G. H. (1977) Biochim. Biophys. Acta, 492, 254-259. Ridordan, J. F., McElvany, k. D., and Borders, C. L. JR. (1977) Science, 195, 884-886. Robbins, K. C., Bernabe, P., Arzadon, D., and Summaria, D. (1973) J. Biol. Chem. 248, 1631. Roberts, M. F., Deems, R. A., Mincey, T. C., and Dennis, E. A. (1977a) J. Bio1. Chem. 252, 2405-2411. Roberts, M. F., Deems, R. A., and Dennis, E. A. (1977b) J. Biol. Chem. 6011-6017. Roberts, M. F., Deems, R. A., and Dennis, E, A. (1977c) Proc. Nat1. Acad. Sci. 74, 1950-1954. Roch, C. O., and Snyder, F. (1975) J. Bio1. Chem. 250, 6564-6566. Saito, K., and Hanahan, D. J. (1962) Biochemistry, l, 521-532. Salach, J. L, Seng, R., Tisdale, H., and Singer, T. P. (1971) J. Biol. Chem. 246, 340-347. Samesjima, Y., Iwanaga, S., Suzuki, T. (1974) F. E. B. S. Lett. 47, 41, 348-351. Sanger, F., and Tuppy, H. (1951) Biochem. J. 49, 463. Sasaki, T., Abrams, B., and Horecker, B. L. (1975) Anal Biochem. 65, 396-403. Scoffone, E., Fontana, A., and Rocchi, R. (1968) Biochemistry, 7, 971-979 Scoffone, E., Jori, G., and Galiazzo, G. (1970) in “Chemical Reactivity and Biological Role of Functional Groups in Enzymes”, Smellie, R. M. S. ed. pp 163-170. Shaw, J. O., Roberts, M. F., Ulevitch, R. J., Henson, P., and Dennis, E. A. (1978) Am. J. Pathol. 91, 517-530. Shechter, Y., Burstein, Y., and Patchornik, A. (1975) Biochemistry, 14, 4497-4503. Shier, W. T., and Trotter, J. T. (1978) Anal. Biochem. 87, 604-611. Shiloah, J., Klibansky, C., Devies, A., and Berger, A. (1973a) J. Lipid Res. 14, 267-278. Shiloah, J., Klibensky, C., and Devies, A. (1973b) Toxicon, 11, 491-497. Shipolini, R. A., Callewaert, G. L., Cottrell, R. C., Doonan, S., and Vernon, C. A. (1971) Eur. J. Biochem. 20, 459. Shipolini, R. A., Callewaert, G. L., Cottrell, R. C., and Vernon, C. A. (1974) Eur. J. Biochem. 48, 465-476. Shriner, R. L., Fuson, R. C., Curtin, D. Y. (1964) “Systematic Identification of Organic Compounds”. Simpson, R. J., Neuberger, M. R., and Liu, T. Y. (1976) J. Biol. chem., 1936-1940. Singleton, W. S., Gray, M. S., Brown, M. L., White, J. L. (1965) J. Am. Oil Chemist’s Soc. 42, 53-56. Slegers, J., Simon, J., Brisbois, L., Peeters, J., and Gillo, L. (1968) J. Chromatogr. 36, 241-243. Slotboom, A. J., Jansen, E. H. J. M., Vlijm, H., Pattus, F., deAraujo, P. S., and deHaas, G. H. (1978) Biochemistry, 17, 4593-4600. Small, D. M., (1971) in “The Bile Acids”, Vol. 11, Chapter 8 (C Nav, P. P. ed.). Sokolovsky, M., Riordan, J. F., vallee, B. L. (1967) Biochem. Biophys. Res. Commun. 27, 20-25. Spackman, D. H., Stein, W. H., and Moore, S. (1958) Anal. Chem., 1190-1206. Spies, J. R., and Chamber, P. C. (1959) Anal. Chem. 21, 1249. Strong, P. N., Goerke, J., Oberg, S. G., and Kelly, R. B. (1976) Proc. Natl, Acad. Sci., U. S. A. 73, 178-182. Tanford, C. (1962) Adv. Prot. Chem. 17, 69-165. Tchorbanov, B., Grishin, E., Aleksiev, B., and Ovchinnikor, Y. (1978) Toxicon, 16, 37-44. Tsuchiya, Y. (1937) Bull. Agr. Chem. Soc. , Japan, 13, 23. Vallee, B. L., and Riordan, J. F. (1969) Ann. Rev. Biochem. , 733-794. VanDam-Mieras, M. C. E., Slotboom, A. J., Pieterson, W. A., and deHaas, G. H. (1975) Biochemistry, 14, 5387-5394. VanDeenen, B. B. M., and deHaas, G. H. (1963) Biochim. Biophys. Acta, 70, 538-553. VanHolde, ,K. E. (1971) Physical Biochemistry, Prentice-Hal1, Inc. Vanwezel, F. M., Slotboom, A. J., and deHaas, G. H. (1976) Biochim. Biophys. Acta, 452, 101-111. Verger, R., Kieras, M. C. E., and deHaas, G. H. (1973) J. Biol. Chem. 248, 4023-4034. Viljoen, C. C., and Botes, D. P. (1975) Toxicon, 13, 343-351. Viljoen, C. C., Visser, L., and .Botes, D. P. (1976) Biochim. Biophys. Acta, 438, 424-436. Viljoen, C. C., visser, D., and Botes, D. P. (1977) Biochim. Biophys. Acta, 483, 107-120. Volwerk, J. J., Pieterson, W. A., and deHaas, G. H. (1974) Biochemistry, 13, 1446-1454. Waku, K., and Nakazawa, Y. (1972) J. Biochem. 72, 149-155. Welcher, F. J. ed. (1963) “Standard Methods of Chemical Analysis”, vol. IIA, pp 930. van Nostrand Reinhold Co. Wells, M. A. (1971) Biochim. Biophys. Acta, 248, 80-86. Wells, M. A. (1972) Biochemistry, 11, 1030-1041. Wells, M. A. (1973a) Biochemistry, 12, 1080-1085. Wells, M. A. (1973b) Biochemistry, 12, 1086-1093. Wells, M. A. (1974) Biochemistry, 13, 2265-2248. Wells, M. A., and Hanahan, D. J., (1969) Biochemistry, 1, 521-532. Westhead, E. W. (1965) Biochemistry, 4, 2139. Whitney, P. L., and Brandt, H. (1976) J. Biol. Chem. 251, 3862. Willadsen, P., deJersy, J., and Zerner, B. (1973) Biochem. Biophys. Res. Commun. 51, 620. Woelk, H., Peiler-Ichikawa, K. (1974) F. E. B. S. Lett. 45, 75-78. Wu, T. W., and Tinker, D. O. (1969) Biochemistry, 8, 1558. Yamamoto, S., Nakanishi, K., Matsuno, R., and Kamikubo, T. (1979) Agric. Biol. Chem. 43, 2499-2506, 2507-2513. Zhelkovskii, A. M., Apsalon, U. R., D’yakov, v. L., Ginodman, L. M., Miroshnikov, A. I., Antonov, V. K. (1977) Bioorg. Khim. 3, 1430-1432. 4, 1665-1672. Yang, C. C., King, K. (1980a) Toxicon, in press. Yang, C. C., King, K. (1980b) Biochim. Biophys. Acta. in press. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/76356 | - |
dc.description.abstract | Phospholipase A2 from the venom of Formosan Cobra (Naja naia atra) has been inactivated by p-bromophenacyl bromide (BPB) and histidine-47 is proposed to be the primary site of modification, based on amino acid analysis. The inactivation by BPB showed many aspects of active site properties so that His-47 is suggested to be in this region. Other alkylating agents (iodoacetic acid, iodoacetamide, and methyl iodide) failed to affect the enzymic activity. Diethylpyrocarbonate-(Ethoxyformic anhydride) and tetranitromethane inactivated the PLA by modification of one or more tyrosine residues. Sulfenylation of tryptophan residues by 2'-nitrophenylsulfenyl chloride also inactivated this enzyme, suggesting that both aromatic residues are essential for the enzymic activity. Methionine residue is hard to be oxidized by Chloramine-T. Other residues are discussed based on the previous results. Finally, several models are compared and summarized as follows: the enzyme binds one calcium ion and a conformational change occurs to expose some functional groups to effect substrate binding. Ca2+-enzyme complex will then bind to micelle produced by phospholipid sad sodium deoxycholate or other detergents. Catalysis occurs through many driving forces and stabilizing forces on substrate molecule with the release of fatty acid and lysophosphatide. | en |
dc.description.provenance | Made available in DSpace on 2021-07-01T08:20:38Z (GMT). No. of bitstreams: 0 Previous issue date: 1980 | en |
dc.description.tableofcontents | @Summary in Chinese(中文摘要)------------------------------(i) @Acknowledgement-----------(vii) @List of Tables----------------(viii) List of Figures---------------------(ix) List of abbreviations--------------(xi) I Chapter 1 Introduction----------------1 1. Phospholipase A2-------------------1 distribution actions importance 2. Chemical modification------------2 concept of active site and other related terms general procedure properties of an ideal reagent 3. Previous results and the purpose of this study--------------5 II Chapter 2 Materials and general procedures------------------11 1. Materials 2. General procedures-------------16 Amino acid analysis and detections-----------16 Chromatography---------------------21 gel filtration ion-exchange chromatography paper chromatography Circular dichroism measurement--------------23 Electrophoresis---------------------25 paper electrophoresis disc polyacrlamide gel electrophoresis Enzymic assay----------------------26 Spectrophotometric titration-------------------27 3. Appendix: Synthesis and purification of histidine derivatives---------------28 III Chapter 3 Isolation and purification of phospholipase A2-------30 Chapter 4 Histidine residue in PLA------------38 1. Special properties of imidazole and its participation in enzymic catalysis-------------------38 2. Chemical modification of histidine residue in PLA-------40 modification with p-bromophenacyl bromide-------------------42 modification with other alkylating agents-----------------------57 3. Summary : Active site around histidine residue in PLA---60 Chapter 5 Aromatic residues in PLA-----------62 1. Consideration of tyrosine residues-----------62 the reaction of diethylpyrocarbonate with PLA----------------62 spectrophotometric titration of PLA------------70 modification with tetranitromethane------------70 2. Consideration of tryptophan residues--------------------------77 modification with 2'-nitrophenylsulfenyl chloride-------------77 Chapter 6 Other residues in PLA----------------83 1. Serine residues---------------------83 2. Cysteine residues and disulfide bridges-----------------------83 3. Amino groups----------------------84 4. Arginine residues-----------------86 5. Carboxyl groups-------------------87 6. Methionine residue---------------87 7. Summary----------91 IV Chapter 7 General discussions-------------------92 1. Specificity of phospholipase A2---------------92 positional specificity substrate specificity 2. Mechanism of ester hydrolysis-----------------93 3. Requirements for the explanation of PLA action-------------95 4. Models proposed up to now--------------------95 5. Overview of chemical modification----------104 @Summary--------------------------105 @References-------------------------106 | |
dc.language.iso | zh-TW | |
dc.title | 臺灣飯匙倩蛇毒中磷脂?甲之化學修飾 | zh_TW |
dc.title | Chimical Modification of Phospholipase A2 from the venom of Formosan Cobra(Naja naja atra) | en |
dc.date.schoolyear | 68-2 | |
dc.description.degree | 碩士 | |
dc.relation.page | 113 | |
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 |
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