The Journal of Natural Sciences (자연과학논문집)
- Volume 14 Issue 2
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- Pages.67-82
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- 2004
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- 1225-6196(pISSN)
Purification and characterization of TPx from archeabacteria, Halococcus agglomeratus
고염 원시박테리아(Halococcus agglomeratus)에 존재하는 TPx 분리 및 생화학적 특성연구
- Choi, Yong-Soo (Department of Biochemistry, Paichai University) ;
- Cha, Mee-Kyung (Department of Biochemistry, Paichai University) ;
- Kim, Il-Han (Department of Biochemistry, Paichai University)
- Published : 2004.08.30
Abstract
A thiol-specific antioxidant protein (TSA or TPx) was purified from Halophilic archeabacteria Halococcus agglomeratus, by DEAE-Cellulose, Phnyl, sepharose, Sephadex G-75, Sephacryl S-100, Sephacryl S-200, and Q-Wepharose FF. This protein exhibited the preventeive effect against the inactivation of glutamine synthehase (GS) activity was support by a thiol-reducing equicalent such as dithiothreitol. TPx activity was maximal at NaCl concentration above 500mM. The molecular mass of the protein was determinated to be 22-kDa by SDS-PAGE. The TPx purified from Halococcus agglomeratus seems to be similar to other TPx family, except for the salt requirement for the maximal antioxidant activity.
고염에서 자라는 원시 박테리아인 Halococcus agglomeratus에서 Thiol-specific antioxidant 활성을 보이는 분자량이 22-kDa인 향산화 단백질을 순수 분리 정제하여 향산화 활성의 특성을 조사하였다. 그 결과 진핵 세포의 Thiol-specific antioxidant protein (TSA of TPx)과 유사한 활성을 갖는 것을 확인 할 수 있었다. 정제된 Thiol-specific antioxidant protein 은 환원제로 thiol 성분을 갖는 비효소적 금속 촉매 산화계(
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