DSpace at EWHA: Studies on the ornithine aminotransferase from sebastes (pteropodus) hubbsi

Browse

My Repository

DSpace at EWHA일반대학원 화학·나노과학과 Theses_Master

View : 1042 Download: 0

Full metadata record

DC Field	Value	Language
dc.contributor.advisor	권동숙	-
dc.contributor.author	한성옥	-
dc.creator	한성옥	-
dc.date.accessioned	2016-08-26T03:08:29Z	-
dc.date.available	2016-08-26T03:08:29Z	-
dc.date.issued	1985	-
dc.identifier.other	OAK-000000014705	-
dc.identifier.uri	https://dspace.ewha.ac.kr/handle/2015.oak/196450	-
dc.identifier.uri	http://dcollection.ewha.ac.kr/jsp/common/DcLoOrgPer.jsp?sItemId=000000014705	-
dc.description.abstract	Sebastes(pteropodus) hubbsi에서 Drnithine aminotransferase를 열처리, (NH_(4))_(2)SO_(4) 분획 분리, DEAE-cellulose chromatography, Sephadex G-200 filtration 법을 사용하여 부분 정제하였다. 이 효소의 마지막 단계의 회수율이 10.7였으며 약30배 정제되었으나 폴리아크릴아마이드 젤 영동법에 의하여 단일단백질로 정제되지는 않았다. 이 효소는 간 세포의 마이토콘드리아 부분에 대부분이 존재함이 밝혀졌다. L-오르니틴과 α-케토글루타레이트에 대한 ㎞값은 각각 0.667mM과 1.829mM이었으며 최적 pH와 온도는 7.3과 3.7℃임이 밝혀졌다.;Ornithine aminotransferase (EC 2.6.1.l3., OAT) was partially purified from sebastes(pteropodus) hubbsi by heat treatment, ammonium sulfate fractionation, DEAE-cellulose chromatography, and gel filtration on Sephadex G-200. The enzyme was partially purified about 30-fold with 10.7% recovery. OAT was found to be located almost in the mitochondrial fractions of the liver cell. The Michaelis constants for ornithine and α-Ketoglu-tarate were found to be 0.667mM and 1.829mM, respectively. Optimum pH and temperature were found to be7.3 and 37℃.	-
dc.description.tableofcontents	CONTENTS = Ⅵ ABSTRACT = Ⅶ Ⅰ. INTRODUCTION = 1 Ⅱ. MATERIALS AND METHODS = 4 A. MATERIALS = 4 B. METHODS = 4 1. Assay of OAT = 4 2. Enzyme Unit = 5 3. Protein Determination = 5 4. Preparation of crude extract = 5 5. Partial Purification of OAT = 6 a) Heat treatment = 6 b) (NH_(4))_(2)SO_(4) fractionation = 6 c) DEAE-celluLose chromatography = 6 d) Gel filtration on Sephadex G-200 = 6 6. Effect of pH on OAT = 7 7. Effect of Temperature and time on OAT = 7 8. Kinetic parameters = 7 Ⅲ. RESULTS = 8 A. PARTIAL PURIFICATION OF OAT = 8 B. INTRACELLULAR LOCALIZATION OF OAT = 8 C. EFFECT OF pH ON OAT = 8 D. EFFECT OF TEMPERATURE AND TIME ON OAT = 14 E. KINETIC PARAMETERS = 14 F. THERMAL STABILITY = 14 G. STABILITY OF THE ENZYME = 14 Ⅳ. DISCUSSION = 19 Ⅴ. CONCLUSION = 21 BIBLIOGRAPHY = 22 국문초록	-
dc.format	application/pdf	-
dc.format.extent	737093 bytes	-
dc.language	kor	-
dc.publisher	이화여자대학교 대학원	-
dc.subject	ornithine	-
dc.subject	aminotransferase	-
dc.subject	sebastes	-
dc.subject	pteropodus	-
dc.subject	hubbsi	-
dc.title	Studies on the ornithine aminotransferase from sebastes (pteropodus) hubbsi	-
dc.type	Master's Thesis	-
dc.title.translated	sebastes (pteropodus) hubbsi의 ornithine aminotransferase에 관한 연구	-
dc.format.page	32 p.	-
dc.identifier.thesisdegree	Master	-
dc.identifier.major	대학원 화학과	-
dc.date.awarded	1985. 2	-