Paberit M, Peips M, Aaviksaar A
Biochim Biophys Acta. 1984 Sep 25;789(3):257-65. doi: 10.1016/0167-4838(84)90181-x.
The influence of inorganic salts on the trans-cinnamoyl-chymotrypsin deacylation kinetics at 25 degrees C and various pH values has been studied: KCl (pH 6.0-13.4), CsCl (pH 9.8 and 13.1), NaCl and Na2SO4 (pH 9.8). Each salt was found to accelerate the reaction with different effectiveness which depended upon pH. The data show that the acyl-enzyme occurs in two forms, which are seen kinetically by different salting effects in deacylation; the equilibrium between the forms is controlled by an ionizing group in the enzyme with pKa about 12.
研究了25℃及不同pH值下无机盐对反式肉桂酰-胰凝乳蛋白酶脱酰动力学的影响：KCl（pH 6.0 - 13.4）、CsCl（pH 9.8和13.1）、NaCl和Na₂SO₄（pH 9.8）。发现每种盐以不同的效率加速反应，这取决于pH值。数据表明酰基酶以两种形式存在，在脱酰反应中通过不同的盐析效应在动力学上可见；这两种形式之间的平衡由酶中pKa约为12的一个电离基团控制。
