학술논문
Purification and Properties of Thioredoxin-I from Cryptococcus neoformans
이용수 5
- 영문명
- Purification and Properties of Thioredoxin-I from Cryptococcus neoformans
- 발행기관
- 강원대학교 기초과학연구소
- 저자명
- Jae-Hoon Sa Chang-Jin Lim
- 간행물 정보
- 『기초과학연구』제9집, 87~102쪽, 전체 16쪽
- 주제분류
- 자연과학 > 자연과학일반
- 파일형태
- 발행일자
- 1998.12.01
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국문 초록
영문 초록
Thioredoxin-I(Trx-I) was partially purified from Cryptococcus neoformans by procedures including heat treatment, DEAE-cellulose ion exchange chromatography, gel filtration on Sephadex G-50, and Q-Sepharose ion exchange chromatography. Its molecular weight is 16.3 kDa protein, which is relatively larger than most known thioredoxins. However, this enzyme is very heat-stable protein. The C. neoformans thioredoxin-I shows a 176-fold lower catalytic efficiency than E. coli thioredoxin when E. coli thioredoxin reductase was used as a reducing enzyme. Further studies should be doe to elucidate the precise role of thioredoxin-I from C. neoformans.
목차
Introduction
Materials and Methods
Results and Discussion
References
키워드
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