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Studies on the ornithine aminotransferase from sebastes (pteropodus) hubbsi

Title
Studies on the ornithine aminotransferase from sebastes (pteropodus) hubbsi
Other Titles
sebastes (pteropodus) hubbsi의 ornithine aminotransferase에 관한 연구
Authors
한성옥
Issue Date
1985
Department/Major
대학원 화학과
Keywords
ornithineaminotransferasesebastespteropodushubbsi
Publisher
이화여자대학교 대학원
Degree
Master
Advisors
권동숙
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℃.
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일반대학원 > 화학·나노과학과 > Theses_Master
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