Cléry C, Renault F, Masson P
Centre de Recherches du Service de Santé des Armées, Unité de Biochemie, La Tronche, France.
FEBS Lett. 1995 Aug 21;370(3):212-4. doi: 10.1016/0014-5793(95)00787-a.
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.
通过压力下的凝胶电泳和8-苯胺基-1-萘磺酸盐（ANS）结合，研究了压力对人丁酰胆碱酯酶结构的变性作用。结果发现，在0.5至1.5千巴的压力下，结合的ANS荧光强度增加，并且当施加约1.5千巴的压力时，酶的流体力学体积膨胀。这些发现表明，丁酰胆碱酯酶的压力变性是一个多步骤过程，并且观察到的瞬时压力变性状态具有熔球的特征。
