期刊论文详细信息
FEBS Letters
Pressure‐induced molten globule state of cholinesterase
Masson, P.1  Renault, F.1  Cléry, C.1 
[1] Centre de Recherches du Service de Santé des Armées, Unité de Biochemie, 24, avenue des Maquis du Grésivaudan, Boîte Postale 87, 38702 La Tronche Cédex, France
关键词: Cholinesterase;    Molten globule;    Pressure;    Electrophoresis;    AChE;    acetylcholinesterase;    BuChE;    butyrylcholinesterase;    MG;    molten globule;    ANS;    8-anilino-1-naphtalene-sulfonate;   
DOI  :  10.1016/0014-5793(95)00787-A
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

The denaturing effect of pressure on the structure of human butyrylcholinesterase was examined by gel electrophoresis under pressure and by 8-anilino-1-naphthalene sulfonate (ANS) binding. It was found that the fluorescence intensity of bound ANS is increased by pressure between 0.5 and 1.5 kbar and that the hydrodynamic volume of the enzyme swells when pressures around 1.5 kbar are applied. These findings indicate that pressure denaturation of butyrylcholinesterase is a multi-step process and that the observed transient pressure-denatured states have characteristics of molten globules.

【 授权许可】

Unknown   

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