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蛋白质盐析动力学:硫酸铵沉淀酵母酶

The kinetics of protein salting-out: precipitation of yeast enzymes by ammonium sulfate.

作者信息

Foster P R, Dunnill P, Lilly M D

出版信息

Biotechnol Bioeng. 1976 Apr;18(4):545-80. doi: 10.1002/bit.260180408.

Abstract

Protein solubility can be adequately represented by the classical Cohn equation for the salting-out of alcohol dehydrogenase and fumarase from clarified yeast homogenate with ammonium sulfate. However, the constant beta in this equation is a function of the contacting procedure employed. The kinetics of continuous salting-out were similar for alcohol dehydrogenase and fumarase. The overall rate equation for precipitation had a variable order which was high initially, up to 3.1, but approached unity on completion of precipitation. This was followed by a partial resolution stage which was first order with respect to the concentration driving force. Precipitate particle size was estimated as 0.5 to 5 mum with continuous flow precipitation producing the largest particles.

摘要

蛋白质溶解度可以用经典的科恩方程来充分描述,该方程用于从澄清的酵母匀浆中用硫酸铵盐析乙醇脱氢酶和富马酸酶。然而,该方程中的常数β是所采用的接触程序的函数。乙醇脱氢酶和富马酸酶的连续盐析动力学相似。沉淀的总速率方程具有可变的级数,最初较高,可达3.1,但在沉淀完成时接近1。随后是一个部分溶解阶段,该阶段相对于浓度驱动力是一级的。连续流沉淀产生的沉淀颗粒尺寸估计为0.5至5微米,产生的颗粒最大。

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