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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.author | Geen-Dong Chang | en |
| dc.contributor.author | 張震東 | zh_TW |
| dc.date.accessioned | 2021-07-01T08:11:24Z | - |
| dc.date.available | 2021-07-01T08:11:24Z | - |
| dc.date.issued | 1980 | |
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Separation et reassociation des sous-unites do l’hormone gonadotrope d'un Poisson Teleosteen, la Carpe ( Cyprinus carpio L.).C. R. Acad. Sc. (Paris), 279 D, 1681-1684. Burzawa-Gerard, E., Goncharor, B. F., and Fontaino, Y. A. ( 1975 ). L’hormone gonadotrope hypophysaire d'un poisson chondrosteen, l’esturgeon (Acipenser stellatus P. ). II. Proprietes biochimiques.Gen. Comp. Endocrinol.27,296-304 Burzawa-Gerard, E., Goncharov, B., Dumas, A., and Fontaine, Y. A.( 1976 ). Further biochemical studies on carp gonadotropin ( cGTH ); biochemical and biological comparison of cGTH and a gonadotropin from Acipenser stellatus P. ( Chondrostei ).Gen. Comp. Endoorinol. 29,498-505. Burzawa-Gerard, E., and Fontaine, T. A. ( 1976 ). Formation d'une molecule bybride dou?e d'une activit? gonadotrope sur la grenouille, A partir de la sous-unit? de l’hormone gonadotrope d’un poisson tele?st?en.C. R. Acad. Sci. Paris Sor. D 282, 97-100. Chang, Y.S., Huang, F. L. 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B.( 1975 ).Primary amino acid sequence of TSR from human pituitary glands. J. Biol. Chem. 250, 6735-6746. Reichert. Jr, L. E. ( 1972 ). Biological studies on the relatedness of subunits of human follicle stimulating hormone and chorionic gonadotropin. Endo. 90, 1119-1122. Sairam, M. R., and Li, C. H.( 1974 ). A simple procedure for separating the subunits of ovine and bovine pituitary interstitial cell stimulating hormone. Arch. Biochom. Biophys. 165, 709-714. Sorimachi, K., and Condliffe, P. G. ( 1978 ). The dissociation of b-TSR. Int. J. Peptido Protein Res. 12, 1-6. Sumpter, J. R., Follett, B. K., and Dodd, J. M. ( 1978 ). Studies on the purification of gonadotropin from dogfish ( Scyliorchinus canicula L. ) pituitary glands. Ann. Biol. aniin. Biooh. Biophys. 18, 787-791. Swaminathan, N., and Bahi, 0. P. ( 1970 ). Dissociation and recombination of the subunits of human chorionic gonadotropin. Biochem. Biopbys. Roe. Commun. 40, 422-427. Tager, H., and Steiner, D. F. ( 1974 ). Peptide hormones.Ann. Rev. Biochem. 43, 509-538. Wober, K., and Osborn, N. M. ( 1969 ).The reliability of molecular weight determination by sodium dodecyl. sulfate-polyacrylamide gel electrophoresis.J. Biol. Chem. 244, 4406-4412. Woods, K. R., and Wang, K. T. ( 1967 ).Separation of daneyl-amino acids by polyamide layer chromatography.Biochm. Biophys. Acta. 133, 369-370. aminathan, N., and Bahl, 0. P. ( 1970 ). Dissociation and reconibination of the subunits of human chorionic gonadotropin. Biochem. Biophys. Res. Commun. 40, 422-427. ger, H., and Steiner, D. F. ( 1974 ).Poptide hormones.Ann. Rev. Biochem. 43, 509-538. ber, K., and Osborn, M. M. ( 1969 ). The reliability of molecular weight determination by sodium dodecyl. sulfate-polyacrylamide gel electrophoresis.J. Biol. Chem.244, 4406-4412. ods, K. R., and Wang, K. T. ( 1967 ).Separation of daxisyl-amino acids by polyamide layer chromatogiaphy.Biochim. Biophys. Acta. 133,369-370. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75018 | - |
| dc.description.abstract | 腦下腺能分泌多種蛋白?激素。這些激素在哺乳類?已被研究得相當透徹，其中三種激素由於結構上除蛋白?本體外仍具有相當量的醣類組成而被稱為醣蛋白激素。它們是甲狀腺刺激素的主要功能是刺激性腺的生長為性腺刺激素。在哺乳類所有被研究過取醣蛋白激素都表示出它們是由二個結構亦為醣蛋白的次單元所組成。這兩個次單元是以及非鍵結合，氫鍵、離子鍵以及嫌水作用被結合的因素。若把醣蛋白激素置於能破壞氫鍵、離子鍵或嫌水作用的惡性條件時，二個次單元就會被解體。 欲研究醣蛋白激素功能與結構的關係，我們必需先分離醣蛋白激素以及其次單元。在哺乳類的研究發現醣蛋白激素可被8M濃度之尿素、1M濃度之丙酸、6M濃度之guanidinium以及丞酸條件解體後二個次單元分手就可運用不同之操作將它們分離純化。曾被成功地運用的操作有：分子篩濾管柱層析、離子交換層析、選擇性沉澱、多重逆流液相分配以及嫌水性親和管柱層析。方法之選擇端視次單元化學性?的差異而求對策。 魚類激素的研究起步較晚，至今祇有少數幾種魚類的性腺刺激素被分離出；即鯉、鱒、鮭、及吳郭魚等。所以魚類性腺刺激素的結構，功能所知仍然有限。?了探討魚類性腺刺激素的結構、功能以及作比較內分泌學的研究。近年來本實驗室著手海鰻腦下腺性腺刺激素的純化以及化學性狀的研究，已經成功地分離得性腺刺激素。本碩士論文的實驗承先?後，目標?海鰻性腺刺激素次單元之純化及化學性狀研究。 二、分離純化之操作： 將新鮮海鰻頭蓋骨剖開，跳出腦下腺，以及超音波振盪便腦下腺搗碎。?冷凍幹燥後即可保存。分離純化之進行首先採取Hartree氏抽取方法將組織中的醣蛋白分子選擇性地抽取出來。最後通過DEAE-celluolse離子交換管柱分離性腺刺激素。經名種性腺刺激素導一的生物測定法以及生化分析方法，我們確定已將海鰻性腺刺激性純化，其結構具有形哺乳類性腺刺激素共同的特性，即胺基酸組成有雷同之處。 將純化的海鰻性腺刺激素以1M濃度之丙酸35℃下培育24小時即可使兩個次單元解體，最後將其通過DEAE-celluolse離子交換管柱，可將二次單元分離、純化。但是這個操作之回收率頗低（11％），所以我們再發展出一個新的分離方法，即是以phenyl-Sepharos 取代DEAE-cellulose.解體後之性腺刺激素迨除去丙酸後通入phenyl Sepharose(以0.1N水性程度不同；次單元Ⅰ毫不停滯而次單元Ⅱ具較大嫌水性而被滯留。待次單元Ⅰ巳全流出管柱後，我們提高沖洗液之酸驗度（0.1炭酸氫氨）沖洗。回收率高達80％。兩個次單元的一些性狀分述如下： （1）.生物性狀： 兩個次單元單獨存在時不具有性腺刺激素的功能，若把它們放在一起培育即可恢復原先之組合進而恢復生物功能。本實驗發現如比得到之組合其生物功能之表現幾乎與原先分子相等，表示分離地過程中次單元並未受到損壞。 （2）免疫性狀： 將純化之次單元注射免子引發得抗體血清。二個次單元在洋菜膠雙重免疫擴散檢定並無交替反應發生，因此它們和結構並無相同之處；此外此點事實意味著它們的純度很高。 （3）化學性狀: 此項實驗我們作了胺基酸組成分析、醣類組成分析、膠體電泳分析以及氮端胺基酸分析。兩個次單元文化學性狀相去甚遠。 三．結論: 由於本實驗成功地純化出海鰻性腺刺激素之次單元，便我們更確信魚類性腺刺激素亦是由二個次單元組成。同時我們還發現海鰻性腺刺激的次單元Ⅰ與哺乳類的次單元則與哺乳類的次單元組雷同哺乳類的β次單元相似。演化過程中它們的結構有很多部分被保留下來。 | zh_TW |
| dc.description.abstract | This study was aimed to purify and oharacterise the subunits of pike eel gonadotropin ( pGTH ). After dissociation with 1 M propionie acid, the subunits of pGTH can be successfully purified by chromatography on Phenyl-Sepharose. The chemical compositions of pGTH subunit I and II were strikingly different. The amino acid composition of subunit I shared a certain degree of homology to that of α subunit of mammalian GTH and subunit II to that of β subunit. Almost full GTH activity could be restored when two sub-inits were reassociated. | en |
| dc.description.provenance | Made available in DSpace on 2021-07-01T08:11:24Z (GMT). No. of bitstreams: 0 Previous issue date: 1980 | en |
| dc.description.tableofcontents | 1. Summary………………………………………………………1 2. Introduction………………………………………………………2 3. Materials and methods……………………………3 A. Chemicals…………………………………………………………5 B. Important instruments………………………6 C. Source of pituitary glands……………………6 D.Purification of pike eel GTH………………………………………………………7 E.Purification of pGTH subunits………………………………………………………9 F. Bioassay of GTH activity by the stimulation of androgen production of carp testis in vitro……10 G. Reassociation of subunits of GTH………………………………………………………12 H.Disc gel eloctrophoresis…………………………………………………………13 I. SDS-gel electrophoresis………………………………………………………………13 J. Quantitation of protein content……………………………………………………………14 K. Amino acid comosition analysis…………………………………………………………………15 L.N-terminal amino acid analysis………………………………………………………15 M. Determination of sialio acid, hexosamines and neutral sugars……………………………………………16 N. Immunization……………………18 0. Immunodiffusion………………………………………………………………19 4. Results: A. Purification of pGTH……………………………………………………………20 B. Purification of pGTH subunits…………………………………………26 C. Reaseociation of pGTH subunits………………………………33 D. Immunological properties of subunit I and II…………………………39 E. Chemical compositions of pGTR subunits………………………………43 5. Discussion…………………………………………45 6. Summary in Chinese……………………………………51 7. Acknowledgements…………………………………57 8. Bibliography………………………58 | |
| dc.language.iso | zh-TW | |
| dc.title | 海鰻腦下腺性腺刺激素次單元之純化及其性質之研究 | zh_TW |
| dc.title | STUDIES ON THE PURIFICATION AND CHARACTERIZATION OF SUBUNITS OF PIKE EEL GONADOTROPIN | en |
| dc.date.schoolyear | 68-2 | |
| dc.description.degree | 碩士 | |
| dc.relation.page | 71 | |
| 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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