http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
- 中文 을 입력하시려면 zhongwen을 입력하시고 space를누르시면됩니다.
- 北京 을 입력하시려면 beijing을 입력하시고 space를 누르시면 됩니다.
RISS 인기검색어
- 검색키워드
- 저자 : 최명언 ( Sung Kwon Chung (검색결과 2 건)
- 무료
- 기관 내 무료
- 유료
-
정성권,최명언,Chung, Sung-Kwon,Choi, Myung-Un 생화학분자생물학회 1985 한국생화학회지 Vol.18 No.3
쥐 뇌의 Monoamine Oxidase (MAO) 단백질에 대한 지질의 작용을 연구하기 위하여 유기용매로 Mitochondria의 지질을 추출해내고 Triton X-100로 MAO를 용해시켰다. Chloroform과 Acetone을 사용했을 때 Mitochondria 전체 지질의 96%를 제거할 수 있었으며 이때 효소 활성도에는 변화가 없었다. 용해된 효소와 인지질을 결합시킴으로써 MAO를 재활성화하였다. 이렇게 재활성화된 MAO의 기본적인 특성을 용해되기 전과 용해된 MAO의 특성들과 비교하였다. Phosphatidylcholine(PC)이 용해된 효소의 활성도를 높였으며 PC와 단백질의 비가 6대 1 일 때 용해되기 전의 활성도의 90%까지 회복되었다. 재활성화된 MAO는 $37^{\circ}C$에세의 안정도가 크게 증가되었고 용해되기 전의 pH, temperature optimum을 회복하였으며, 재활성에 의해 $V_{max}$ 값은 변화가 없었고 $K_m$ 값은 0.18 mM에서 0.12 mM로 변화되었다. 이러한 결과로 볼때 이상과 같은 용해와 재활성화의 실험방법으로써 MAO에서의 지질의 역할에 대한 정보를 얻을 수 있을것으로 여겨지며 단백질과 지질의 상호작용의 특성에 관한 정보를 얻는데 상당한 도움이 될것으로 사려된다. In order to investigate the nature of lipid-protein interactions of monoamine oxidase (MAO) of rat brain, the membrane-bound MAO was solubilized with Triton X-100 after depletion of mitochondria, lipid by organic solvents. Extraction with chloroform and acetone removed 96% of total lipid from mitochondria, while there was no apparent change in enzyme activity. Reactivation was performed by interacting the defined phospholipids with the solubilized MAO. The basic properties of the reactivated enzyme were compared with those of both membrane-bound and solubilized enzyme. It was found that phosphatidylcholine was the activator for the solubilized enzyme with 90% activation at the lipid to protein ratio of 6 to 1. When reactivated the stability of the enzyme improved greatly at $37^{\circ}C$ and the pH optimum of the solubilized enzyme shifted to that of the membrane-bound enzyme. While $K_m$ value of 0.18 mM of the solubilized enzyme altered to 0.12 mM upon reactivation, the value of $V_{max}$ remained unchanged. It seems that this system could provide a series of basic informations on the roles of phospholipids in rat brain MAO and the nature of the interactions between membrane-bound proteins and their environmental phospholipids.
-
지질을 제거한 쥐 뇌의 Monoamine Oxidase 의 용해와 특성 연구
정성권,최명언 ( Sung Kwon Chung,Myung Un Choi ) 생화학분자생물학회 1985 BMB Reports Vol.18 No.3
In order to investigate the nature of lipid-protein interactions of monoamine oxidase (MAO) of rat brain, the membrane-bound MAO was solubilized with Triton X-100 after depletion of mitochondrial lipid by organic solvents. Extraction with chloroform and acetone removed 9696 of total lipid from mitochondria, while there was no apparent change in enzyme activity. Reactivation was performed by interacting the defined phospholipids with the solubilized MAO. The basic properties of the reactivated enzyme were compared with those of both membrane-bound and solubilized enzyme. It was found that phosphatidylcholine was the activator for the solubilized enzyme with 90% activation at the lipid to protein ratio of 6 to 1. When reactivated the stability of the enzyme improved greatly at 37? and the pH optimum of the solubilized enzyme shifted to that of the membrane-bound enzyme. While K_m value of 0.18 mM of the solubilized enzyme altered to 0.12 mM upon reactivation, the value of V_(max) remained unchanged. It seems that this system could provide a series of basic informations on the roles of phospholipids in rat brain MAO and the nature of the interactions between membrane-bound proteins and their environmental phospholipids.
연관 검색어 추천
이 검색어로 많이 본 자료
활용도 높은 자료
