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胃蛋白酶和胰蛋白酶晶体状态热变性的微量量热法

Microcalorimetry of thermal denaturation of pepsin and trypsin in the crystal state.

作者信息

Makarov A A, Esipova N G, Monaselidze D R, Mgeladze G N, Madzhagaladze G V, Kuranova I P, Grebenko A I

出版信息

Biochim Biophys Acta. 1976 May 20;434(1):286-9. doi: 10.1016/0005-2795(76)90060-x.

Abstract

Heating of pepsin and trypsin crystals was studied by scanning microcalorimetry. A sharp decrease in temperature, halfwidth and heat of transition with a decrease in heating rate was discovered. It was shown that thermal transition is connected only with the denaturation of protein molecules in the crystal and not accompanied by the crystal disintegration into separate molecules.

摘要

通过扫描量热法研究了胃蛋白酶和胰蛋白酶晶体的加热过程。发现随着加热速率的降低,温度、半高宽和转变热急剧下降。结果表明,热转变仅与晶体中蛋白质分子的变性有关,而不伴随着晶体分解为单个分子。

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