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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.author | 翟兆平 | zh_TW |
| dc.date.accessioned | 2021-07-01T08:16:35Z | - |
| dc.date.available | 2021-07-01T08:16:35Z | - |
| dc.date.issued | 1993 | |
| dc.identifier.citation | 1. Alpers, D. H. (1969) Seperation and isolatioan of rat and human intestinal beta-galactosidase. J. Biol. Chem. 244, 1238-1246. 2. Aronson, N. N. (1972) in “The Glycoprotein” (Hottschalk, A. ed) PartB, pp1211-1227, Elsevier publishing Co., Amsterdam. 3. Asp, N. G., Dahlqvist, A., and Koldvosky, O. (1969) Human small intestinal beta-galactosidase seperation and cheracterization of one lactase and one hetero beta-galactosidase. Biochem. J. 114, 351-359 4. Asp. N. G., and Dahlgrest, A. (1972) Human small intestine betagalactosidase: specific assay of three different enzymes. Anal. Biochem. 47, 527-538. 5. Berent, S. L., and Radin, N. S. (1981a) Mechanism of activation of glucocerebrosidase by co-beta-glucosidase (glucosidase activator protein) Biochim. Biophys. Acta. 664, 572-578. 6. Berent, S. L., and Radin, N. S. (1981b) Beta-gluco- sidase activator protein from bovine spleen (“co-glucosidase”). Arch. Biochem. Biophys. 208, 248-260 7. Beutler, E., and Kuhl, W. (1970) Detection of the defect of Gaucher’s disease and its carrier state in peripheral-blood leukocytes. Lancet i, 612-613. 8. Burj. J., Conzelmann, E., Sandoff, K., Soloman, E., and Swallow, D. M. (1985) Mapping of the gene coding for the human GM2 activator protein to chromosome 5. Ann. Hum. Genet. 49, 41-45. 9. Cheetham, J. C., Artymiuk, P. J., Philps, D. C. (1992) Refinement of an enzyme complex with inhibitor bound at partial occupance: Hen egg white lysozyme and tri-N-aectylchitotriose at 1. 75A resolution. J. Mol. Biol. 224, 613-628. 10. Cherian, R., and Balasubramanian, A. S. (1980) The characterization of a thermostable activator of beta-D-glucosidase in normal human saliva. Clin. Chem. Acta. 110, 169-175. 11. Christamanou, H., Aignesberger, A., and Linke, R. P. (1986)Immunochemical characterization of two activator proteins stimulating enzymatic sphingomyelin degradation in vitro. Biol. Chem. Hoppe-Seyler 367, 879-890. 12. Chuang, N. -N., Yang, B. -C., and Yeh, C. -C. (1991) Purification and characterization of the shrimp Penaeus japonicus (Crustacea Decapoda). J. Exp. Zool. 259, 26-31. 13. Collard, M. W., Sylvester, S. R., Tsuruta, J. K., and Griswold, M. D. (1988) Biosynthesis and molecular cloning of sulfated glycoprotein-1 secreted by rat setorli cells: sequence similarity with the 70 kilodalton precursor to sulfatide/GM1 activator. Biochem. J. 27, 4557-4564. 14. Conzelmann, E., and Sandhoff, K. (1987) Activator proteins for lysosomal glycolipid hydrolase. Method. Enz. 138, 792-805. 15. Datta, S. C., and Radin, N. S. (1984) Determination of the glucosidase-stimulating proteins by competetive enzyme-linked immunoassay. Anal. Biochem. 142, 196-203. 16. Dawson, R. M. C., Elliott, D. C., Elliott, W. H., and Jhons, K. M. (1986) from “Data for Biochemical Analysis” pp417-448. Clarendon press. Oxford. U. K. 17. Fischer, G., and Jatzkewitz, H. (1978) The activator of cerebroside-suiphatase: a model of activator. Biochim. Biophys. Acta. 528, 69-76. 18. Fluharty, A. L., Katona, Z., Meek, W. E., Frei, K., and Fowler, A. V. (1992) The cerebroside sulphate activator from pig kidney: purification and molecular structure. Biochem. Med. Metabol. Biol. 47, 66-85. 19. Fujibayashi, S., Kao. F. -T., Jonce, C., Morse, H., Law, M., and Wenger, D. A. (1985) Assignment of the gene for human sphingolipid activator protein -2 (SAP-2) to human chromosome 10. Ame. J. Hum. Genet. 37. 741-748. 20. Fujibayashi, S., and Wenger, D. A. (1986) Synthesis and processing of sphingolipid activator protein-2 (SAP-2) in cultured human fibroblast. J. Biol. Chem. 261, 15339-15343. 21. Furst, W., and Sandhoff, K. (1992) Activator proteins and topology of lysosomal sphingolipid catabolism. Biochim. Biophys. Acta. 1126, 1-16. 22. Gatt S. (1966) Enzymatic hydrolysis of sphingolipid: Hydrolysis of monosialoganglioside and hexosylceramide by rat brain beta-galatosidase. Biochim. Biophys. Acta. 137. 192-195. 23. Hajra, A. K., Bowe, D. M., Kishimoto, Y., and N, S. Radin. (1966) Cerebroside galactosidase in brain. J. Lipid. Res. 7, 379-386. 24. Hakomori, S. -i. (1981) Glycosphingolipid in cellular interaction, differentiation, and oncogenesis. Ann. Rev. Biochem. 50, 733-764. 25. Helenius, A., McCaslin, D. R., Fries, E., and Tanford, C. (1979) Properties of detergents. Method. Enzy. 56, 734-749. 26. Henchtman, D., and LeBlanc, D. (1977) Purification and properties of the hexosaminidase A activating protein from human liver. Biochem. J. 167, 693-701. 27. Hineno, T., Sano, A., Kondoh, K., Ueno, S. -i., Kakimoto, Y., and Yoshida, K. -i. (1991) Secretion of sphingolipid activator precursor, prosaposin. Biochem. Biophys. Res. Commun. 176, 668-674. 28. Ho, M. W. (1973) Identity of acid beta-glucosiddase and glucocerebrosidase in human spleen. Biochem. J. 136, 721-729. 29. Ho, M. W., and O’Brien, J. S. (1971) Gaucher’s Disease : Deficiency of acid beta-glucosidase and reconstitution of enzyme activity in vitro. Proc. Natl. Acad. Sci. USA 68, 2810-2813. 30. Inui, K., Emmett, M., and Wenger, D. A. (1983) Immunological evidence for deficiency in an activator protein for sulfatide sulfatase in a variant form of metachromatic leukodystrophy. Proc. Natl. Acad. Sci. USA 80, 3074-3077. 31. Inui, K. Kao, F. -T., Fujibayashi, S., Jones, C., Morse, H. G. Law, H. L., and Wenger, D. A. (1985) The gene coding for a sphingolipid activator protein, SAP-1, is on human chromosome 10. Hum. Genet. 69, 197-200. 32. Inui, K., and Wenger, D. A. (1983) Concentration of an activator protien for sphingolipid hydrolysis in liver and brain samples from patients with lysosomal storage disease. J. Clin. Invest. 72, 1622-1628. 33. Kishimoto, Y., Davies, W. E., and Radin, N. S. (1965)Developing rat brain: changes in cholesterol, galactolipid, and the individual fatty acid of gangliosides and glycerophosphatides. J. Lipid. Res. 6, 532-536. 34. Kondoh, K., Hineno, T., Sano, A., and Kakimoto, Y. (1991) Isolation and characterization of prosaposin from human milk. Biochem. Biophys. Res. Commun. 181, 286-292. 35. Laemmli, U. K. (1970)Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 277, 680-685. 36. Lane, L. C. (1978) A simple method for stabilizing proteinsulfhydryl groups during SDS-gel electrophoresis. Anal. Biochem. 86, 555-669. 37. Li, S. -C., Hirabayashi, Y., and Li, Y. -T. (1981) A protein activator for the enzymatic hydrolysis of GM2 ganglioside. J. Biol. Chem. 256, 6234-6240 38. Li, S. -C., Kihara. H., Serisawa, S., Li, Y. -T., Fluharty, A. L. . Mayers, J. S., and Shapiro, L. J. (1985) Activator protein required for the hydorlysis of cerbroside sulfate: Deficiency in urine of patients affected with cerebroside sulfate activator deficicy and inditity with activators for the enzymatic hydrosis of GM1 gangolioside and globotriao-sylceramide. J. Biol. Chem. 260, 1867-1871. 39. Li, S. -C., Nakamura, T., Ogama, A., and Li, Y. -T. (1979) Evidence for the prescence of two sepsrate protien activators for the enzymatic hydrolysis of GM1 and GM2 ganglioside. J. Biol. Chem. 254, 10592-10595. 40. Li, S. -C., Sonnino, S., Tattamanti, G., and Li, Y. -T. (1988) Charaterization of a nonspecific activator protein for the enzymatic hydrolysis of glycolipid. J. Biol. Chem. 263, 6588-6591. 41. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) Portein measurement with the folin phenol reagent. J. Biol. Chem. 193, 265-275. 42. Mehl, E., and Jatzkewitz, H. (1964) Eine cerebrosidsulfatase aus schwieniere. Hoppe-Seylar’s Z. Physiol. Chem. 339, 260-276. 43. Mehl, E., and Jatzkewitz, H. (1968) Cerebroside-3-sulfate as a physiological substrate of arylsulfatase A. Biochim. Biophys. Acta. 151, 619-627. 44. Merril, C. R., Goldman, D., Sedman, S. A., and Ebert, N. H. (1981)Ultrasensitive stain for proteins in polyacrylamide gels shows regional variation in cerebrospinal fluid proteins. Science. 211, 1437-1438. 45. Morimoto, S., Martin, B. M., Yamamoto, Y., Kretz, K. A., O’Brien, J. S., and kishimoto, Y., (1989) Saposin A: second cerebroside activator protein . Proc. Natl. Acad. Sci. USA 86, 3389-3393. 46. Morimoto, S., Kishimotot, Y., Tomic, J., Weiler, S., Ohashi, T., Barranger, J. A., Kretz, K. A., and O’Brien, J. S. (1990) Interaction of saposins, acidic lipids and glucoceramidase. J. Biol. Chem. 265, 1933-1937. 47. Moromoto, S., Martin B., Kishimoto, Y., and O’Brien, J. S. (1988) Saposin D: a sphingomyelinase activator. Biochem. Biophys. Res. Commun. 156, 403-401. 48. Neugebauer, J. (1990) A guide to the properties and uses of detergents in biology and biochemistry. Calbiochem corporation. 49. O’Brien, J. S., Kretz, K. A., Dewji, N., Wenger, D. A., Esch, F., and Fluharty, A. U. (1988) Coding of two sphingolipid avtivator protiens (SAP-1 and SAP-2) by same genetic locus. Science 241, 1098-1101 50. O’Brien, J. S. (1972) in The Metabolic Basis of Inherited Disease (Stanbury, J. B., Wyngarrden, J. B . and Fredrickson, D. S., eds. ), 3rd ed., Chap. 30, McGraw-Hill, New York. 51. O’Brien, J. S., and Kishimoto, Y. (1991) Saposin proteins :structure, function, and role in human lysosomal storage disorder. FASEB J. 5, 301-308. 52. Paton, B. C., Schmid, B., Kustermann-Kuhn, B., Polous. A., and Harzer, K. (1992) Additional biochemical findings in a patient and fetal sibling with a genetic defect in the sphingolipid activator protein (SAP) precursor, prosaposin. Biochem. J. 285, 481-488 53. Potier, M., Lamontagne, S., Michud, L., and Tranchemontagne, J. (1990) Human nuraminidase is a 60-kDa-processing product of prosaposin Biochem. Biophys. Res. Commun. 173, 449-456. 54. Rafi, M, A., Amini, S., Zhang, X. L., and Wenger, D. A. (1992) Correction of sulfatide metabolism after transfer of prosaposin cDNA to cultured cells from a patient with SAP-1 deficiency. Ame. J. Hum. Genet. 50, 1252-1258. 55. Sakamoto, Y., Kitamura, K., Yoshimura. K., Nishijima, T. and Uyemura, K. (1987) Complete amino acid sequence of P0 protein in bovine peripheral nerve myeline. J. Biol. Chem. 262, 4208-4214. 56. Sano, A., Hineno, T., Mizuno, T., Kondoh, K., Ueno, S. -i., Kakimoto, Y., and Inui, K. (1989) Sphingolipid activator proteins and their precursor. Biochem. Biophys. Res. Commun. 165, 1191-1197 57. Sano, A., Radin, N. S. (1988a) The carbohydrate moeity of the activator protein for the glucocerebroside beta-glucosidase. Biochem. Biopys. Res. Commun. 154, 1197-1203. 58. Sano, A., Radin, N. S., Jhonson, L. L., and Tarr, G. E. (1988b) The activator protein for glucoceramide beta-glucosidase from guinea pig liver improved isolation method and complete amino acid sequence. J. Biol. Chem. 263, 19597-19601. 59. Schlote, W., Harzer, K., Chritomanou, H., Paton, P. C., Kusterman-Kuhn, B., Schmid. B., Seeger, G., Beudt, U., Schuster, I., and Langenbeck, U. (1991) Sphingolipid activator protien-1 deficiency in MLD with normal arylsulfataseA activity. Eur. J. Pediat. 150, 584-591. 60. Schnabel, D., Schroder, M., and Sandoff, K. (1991) Mutation in the sphingolipid activator protein-2 in a patiente with a variant of Gaucher’s disease. FEBS, Lett. 284, 57-59. 61. Schofield, D. E., Scott, C, R., Lage, J. M., and Farrell, D. F. (1992) Gaugher’s disease in the presence of normal glucocerebrosidase activity. Hum. Pathol. 23, 588-592. 62. Sheh. L., Glew. R. H., Bothner-By, A. A., and Mishra, P. K. (1988) High-resolution proton Nuclear Magnetic Resonance studies of the glucocerebrosidase activator protein from Gaucher’s spleen. Biochem. 24, 6645-6651. 63. Sheinblatt, M. (1989) NMR studies on the induced denaturation of lysozyme by guanidine hydrochloride in the presence fo the inhibitor. Biopolymers. 28, 1913-1921. 64. Shigematsu, H., Morimoto, S., Kishimoto, Y., Weiler, S., Tomic, J., Barranger, J., Shinohara, M., Yeager, M., and O’Brien, J. S. (1990) Saposins (sphingolipid activator proteins) in Twitcher mutant mouse. J. Neurochem. 55, 1659-1662. 65 Sloan, H. R. (1987) Ganglioside GM1 beta-galactosidase. Method. Enz. 28, 868-874. 66. Suzuki, K., in “Practical Enzymology of the Sphingolipidosis” (Glew. R. H and Peters, S. P. eds. ), p101 Alan. R. Liss, Inc, New York, 1977. 67. Tayama, M., O’Brien, J. S. and Kishimoto, Y. (1992) Distribution of saposins (sphingolipid activator proteins) in tissues of lysosomal storage disease. J. Mol. Neurosci. 3, 171-175. 68. Tsuda, M. Sakiyama, T., Endo, H., and Kitagawa, T. (1992) The primary structure of mouse saposin. Biochem. Biophys. Res. Commun. 184, 1266-1272. 69. Vaccaro, A. M., Muscillo, M., Gallozzi, E., Savioli, R., Totti, M., and Suzuki, K. (1985) An endogenous activatorprotein in human placenta for enzymatic degradation of glucosylceramide. Biochim. Biophys. Acta. 836, 157-166. 70. Vogel, A., Furst. W., Abo-Hashish, M. A., Lee-Vanpl M. Conzelmann, E., and Sandhoff, K. (1987) Identification of the activator proteins for the enzymatic hydrolysis of sulfatides, ganglioside GM1, and globotriaosylceramide. Arch. Biochem. Biophys. 259, 627-638. 71. Wyckoff, M., Radbord, A., and Chrambach A. (1977) Polyacrylamide gel electrophoresis in sodium dodecylsulphate-containing buffers using multiphasic buffer system. Anal. Biochem. 78, 459-482. 72. Wynn, C. H. (1986) A triple-binding-domain model explains the specificity of the enzymatic hydrolysis of a sphingolipid activator protein (SAP-1) with sulphatides, ganglioside GM1, and globotrio-sylceramide. Biochem. J. 240, 921-924. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75936 | - |
| dc.description.abstract | 利用DE-52陰離子交換管柱，Con A親和力管柱及高效率液相層析逆相碳四管柱（h.p.l.c.RP-C4）可自無脊椎動物斑節蝦肝胰臟中純化出β-半乳糖??的活化蛋白（β-galactosidase activator protein)。此活化蛋白?小分子量（15 kDa)，熱安定（heat stable）的醣蛋白（glycoprotein)，比活性（specific activity)?406 units/mg，較同實驗中由人類胎盤純化的活化蛋白比活性(800 units/mg）低。 在pH4.6的分析緩衝液中，活化蛋白有最佳活性；pH值高於5或低於3.6都不適合活化蛋白的作用。以不同性質（head group電性）介面活性劑（detergent）測試結果指出：在陰離子介面活性劑（anionic detergent）牛磺膽酸鹽（sodium taurocholate）下，活化蛋白活性較強；且最適濃度?0.01％。 本實驗也發現：斑節蝦活化蛋白能加強斑節蝦及jack bean β-半乳糖??的活性；而對α葡萄糖??，β-葡萄糖??沒有作用。其性質與人類saposin B相近，具有專一性（specificity）但無物種間專一性（species specificity）。另外，活化蛋白不影響β-半乳糖??的熱安定性（thermal stability)。 | zh_TW |
| dc.description.abstract | A heat stable, small (apparant molecular mass 15 kDa) glycoprotein was purified as beta-galactosidase activator protein from the hepatopancreas of shrimp Penaeus japonicus with a specific activity of 406 units / mg by using a combination of DE-52 anionic exchange chromatography, Con A chromatography and RP-C4 h.p.l.c. This activator protein stimulates beta-galactosidase activity in a pH range between 3.6 to 5 and has an optimal pH at 4.6. Treatment with various detergents reveals that under anionic detergents such as sodium taurocholate, activator can exert its activity better, and we recommended a concentration of 0.01 %. In our experiment, we found that this activator protein enhances both shrimp and jack bean beta-galactosidase but not alpha-glucosidase or beta-glucosidase which is characteristic for human saposin B. In addition, activator protein shows no effects on the thermal stability of beta-galactosidase. | en |
| dc.description.provenance | Made available in DSpace on 2021-07-01T08:16:35Z (GMT). No. of bitstreams: 0 Previous issue date: 1993 | en |
| dc.description.tableofcontents | 謝辭…………………i 中文摘要……………ii 英文摘要(Abstract)………iii 名詞縮寫表……………………iv 壹、引言………………………1 貳、材料及方法…………………9 參、結果………………………21 肆、討論……………………30 伍、結論………………………36 陸、參考文獻……………37 圖表………………………48 | |
| dc.language.iso | zh-TW | |
| dc.title | 純化並定性斑節蝦Penaeus japonicus 肝胰?中β-半乳糖??的活化蛋白 | zh_TW |
| dc.title | PURIFICATION AND CHARACTERIZATION OF THE β-GALACTOSIDASE ACTIVATOR PROTEIN FROM THE HEPATOPANCREAS OF SHRIMP Penaeus japonicus | en |
| dc.date.schoolyear | 81-2 | |
| dc.description.degree | 碩士 | |
| dc.relation.page | 69 | |
| dc.rights.note | 未授權 | |
| dc.contributor.author-dept | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 動物學研究所 | zh_TW |
| 顯示於系所單位： | 動物學研究所 | |
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