학술논문
Thioltransferase from Arabidopsis thaliana Seed: Purification to Homogeneity and Characterization
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- 영문명
- Thioltransferase from Arabidopsis thaliana Seed: Purification to Homogeneity and Characterization
- 발행기관
- 강원대학교 기초과학연구소
- 저자명
- Young-Wook Cho Joon Chul Kim Chang Duck Jin Tae Jin Han Chang-Jin Lim
- 간행물 정보
- 『기초과학연구』제10집, 149~154쪽, 전체 6쪽
- 주제분류
- 자연과학 > 자연과학일반
- 파일형태
- 발행일자
- 1999.12.01
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국문 초록
영문 초록
Thioltransferase is a general GSH-disulfide reductase of Importance for redox regulation. The protein tbioltransferase has been purified to apparent homogeneity on SDS-PAGE from the Arabidopsis thalina seed. The purification procedures included DEAE-cellulose ion exchange chromatography, Sephadex G-75 gel filtration, Q-Sepharose ion exchange chromatograpby, and DEAE-Sephadex A-25 ion exchange chromatography. The enzyme has a molecular mass of 22 kDa and a pI of 4.8, and it is beatstable. Thc protein bad broad specificities for substrates ranging from low-molecular disulfides (S-sulfocysteine and cystine) to protein disulfides (trypsin and insulin). However, it could not reduce the disulfide linkages of ribonuclease A and bovine serum albumin. It could utilize non-disulfide substrates such as dehydroascorbic acid and alloxan. The protein can reduce the disulfide bond in 2-bydroxyetbyl disulfide with an optimum pH or 8.5. Its activity was greatly activated by monothlol compounds such as reduced glutathione and L-cystelne.
Keyword: Arabidopsis thaliana; Glutaredoxin, Thioltransferase
목차
Introduction
Materials and Methods
Results and Discussion
References
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