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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.author | LIH-CHING HSU | en |
| dc.contributor.author | 許麗卿 | zh_TW |
| dc.date.accessioned | 2021-07-01T08:14:16Z | - |
| dc.date.available | 2021-07-01T08:14:16Z | - |
| dc.date.issued | 1986 | |
| dc.identifier.citation | References 1) Noda, M. et al. Nature 229, 793—797 (1982) 2) Noda, M. et al. Nature 301, 251—255 (1983) 3) Noda, M. et al. Nature 302, 528—532 (1983) 4) Noda, M. et al. Nature 305, 818—823 (1983) 5) Ullrich, A. et al. Nature 309, 418—425 (1984) 6) Ullrich, A. et al. Science 313, 756-761 (1985) 7) Butt, W.R. Hormone Chemistry 2nd ed. vol.1 Protein, Polypeptide and Peptide Hormone, published by Ellis Horwood Limited. 8) Lefkowitz, R.J. (ed.) Receptor Regulation (Receptors and Recognition, series B, vol.13), published by Chapman and Hall in 1981, p.69. 9) Ranke, M.B., Stanley, C.A., Tenore, A., Rodbard, D, Bongiovanni, A.M., Parks, J.S. Endocrinology 99, 1033—1045 (1976) 10) Posner, B.I., Kelly, P.A., Shiu, R., Friesen, H.G. Endocrinology 95, 521—531 (1974) 11) Kelly, P.A., Posner, B.I., Tsushima, T., Friesen, H.G. Endocrinology 95, 532—539 (1974) 12) Posner, B.I., Kelly, P.A., Friesen, H.G. Proc. Nat. Acad. Sci. USA 71, 407—2410 (1974) 13) Shiu, R., and Friesen, H.G. J. Biol. Chem. 249, 7902— 7911 (1974) 14) Das, M., Miyakawa, T., Fox, C.F., Pruss, R.M., Aharonov A., Herschman, H.R. Proc. Nat. Acad. Sci. USA 74, 2790—2794 (1977) 15) Pilch, P.F. and Czech, M.P. J. Biol. Chem. 254, 3375-3381 (1979) 16) Yip, C.C., Yeung, C.W.T., Moule, M.L. Biochem. 19, 70-76 (1980) 17) Greenwood, F.C., Hunter, W.M., Glover, J.S. Biochem. J. 89, 114—123 (1963) 18) Desbuquois, B., Krug, F., Cuatrecasas, P. Biochim. Biophys. Acta 343, 101—120 (1974) 19) Cuatrecasas, P. Proc. Nat. Acad. Sci. USA 69, 318-322 (1972) 20) Tsushima, T., Murakami, H., Wakai, K., Isozaki, O., Sato, Y., Shizume, K. FEBS Lett. 147, 49—53 (1982) 21) Hughes, J.P., Simpson, J.S.A., Friesen, H.G. Endocrinology 112, 1980—1985 (1983) 22) Hughes, J.P., Tanaka, T., Gout, P.W., Beer, C.T., Noble, R.L., Friesen, H.G. Endocrinology 111, 827—832 (1982) 23) Goodman, H.M., and Levy, L.K. Endocrinology 113, 2017-2023 (1983) 24) Postel—Vinay, M.C. FEBS Lett. 69, 137-140 (1976) 25) Fracis, M.J.O., and Hill, D.J. Nature 255, 167—168 (1975) 26) Borst, D.W., and Sayare, M. BBRC 105, 194—201 (1982) 27) Donner, D.B. J. Biol. Chem. 258, 2736—2743 (1983) 28) Gorin, E., and Goodman, H.M. Endocrinology 114, 1279-1286 (1984) 29) Su, C.C., Schwartz, J., Kikuchi, G. J. Biol. Chem. 259, 1099—1104 (1984) 30) Mitani, M. and Dufau, M.L. J. Biol. Chem. 261, 1309-1315 (1986) | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75625 | - |
| dc.description.abstract | 摘要 碘化人類生長激素(125I-hGH)對雌鼠肝臟微小體膜(female rat liver microsomal membranes)有專一性及飽和性之結合。此種結合受時間、溫度及pH之影響，而且與膜蛋白質之濃度呈函數關係。豬激乳素(porcine prolactin)可抑制此125I-hGH與肝臟細胞膜之結合，豬生長激素則否。此結果顯示125I-hGH絕大多數是與泌乳結合位置(lactogenic binding sites)亦即激乳素受體(prolactin receptors)結合。Scatchard plot分析呈直線，亦顯示此為單一結合位置。以disuccinimidyl suberate(DSS)或ethylene glycol bis-succinimidyl succinate (EGS)處理，則專一性結合之125I-hGH可與細胞膜蛋白質聯結，將這些蛋白質以SDS gel electrophoresis展開，結果產生三條具有放射性之bands(分子量相當於41，66及126Kdal)，在沒有DSS或EGS，或者有大量未碘化hGH存在下，並無此結果。由這些資料顯示hGH(21Kdal)與20，45及105Kdal之勝?聯結。這些勝?可能是激乳素受體之次單元(subunits)。 | zh_TW |
| dc.description.abstract | Abstract 125I-hGH was found to show specific and saturable binding to the liver microsomal membranes of the female rat, which was time, temperature and pH dependent and was a function of concentration of membrane protein. It was shown that porcine prolactin but not porcine growth hormone can inhibit the binding of 125I-hGH to the liver membranes. This result suggested that 125I-hGH bind almost exclusively to the lactogenic binding sites (or prolactin receptors). Scatchard analysis produced a linear plot also suggested the presence of single class of binding sites. When treated with DSS or EGS, the specifically bound hGH was cross-linked to membrane proteins. SDS gel electrophoresis revealed three bands of radioactivity (Mr=41,000, 66,000, and 126,000) that were not seen in controls lacking DSS (or EGS) or in the presence of large amount of cold hGH. These data indicated that hGH (Mr=21,000) was cross-linked to peptides of 20, 45, and 105Kdal. These peptides may be the subunits of prolactin receptors. | en |
| dc.description.provenance | Made available in DSpace on 2021-07-01T08:14:16Z (GMT). No. of bitstreams: 0 Previous issue date: 1986 | en |
| dc.description.tableofcontents | 目次 一、中文摘要....................1 二、緒言....................2 三、材料與儀器....................7 四、實驗方法....................9 五、結果....................18 六、討論....................32 七、英文摘要....................36 八、縮寫表....................37 九、參考文獻....................38 十、謝詞....................40 | |
| dc.language.iso | zh-TW | |
| dc.title | 碘化人類生長激素與雌鼠肝臟細胞膜上之受體之專一性結合及聯結 | zh_TW |
| dc.title | Specific Binding and Cross-Linking of Iodinated Human Growth Hormone to the Receptors on Female Fat Liver Membranes | en |
| dc.date.schoolyear | 75-2 | |
| dc.description.degree | 碩士 | |
| dc.relation.page | 43 | |
| 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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