학술논문
Thioltransferase (Glutaredoxin) from Chinese Cabbage: Purification and Properties
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- 영문명
- Thioltransferase (Glutaredoxin) from Chinese Cabbage: Purification and Properties
- 발행기관
- 강원대학교 기초과학연구소
- 저자명
- Young-Wook Cho Eun-Hee Park Chang-Jin Lim
- 간행물 정보
- 『기초과학연구』제9집, 223~229쪽, 전체 7쪽
- 주제분류
- 자연과학 > 자연과학일반
- 파일형태
- 발행일자
- 1998.12.01
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국문 초록
영문 초록
Thioltransferase, also known as glutaredoxin, was purified from Chinese cabbage (Brassica campestris ssp. napus var. pekinensis) by a combination of ion-exchange chromatography and gel filtration. Its purity was confirmed by SDS-polyacrylamide gel electrophoresis and its molecular weight was estimated to be about 12,000 which is comparable with those of most known thioltransferases. The enzyme utilizes 2-hydroxyethyl disulfide, S-sulfocysteine, α-chymotrypsin insulin, and trypsin as substrates in the presence of reduced glutathione. The enzyme has Km values of 0.03-0.97 mM for these substrates. It appeared to contain dehydroascorbate reductase activity. The pH optimum of the enzyme was 8.5, when 2-hydroxyethyl disulfide was used as a substrate. It was greatly activated by reduced glutathione. Its activity was not significantly lost when stored at high temperature, indicating its thermostable character. It may play an important role in thiol-disulfide exchange in plant cells.
목차
Introduction
Materials and Methods
Results and Discussion
References
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