Levison P R, Tomalin G
Biochem J. 1982 Sep 1;205(3):529-34. doi: 10.1042/bj2050529.
At 37 degrees C, human plasma kallikrein I follows Michaelis-Menten behaviour and exhibits a normal linear relationship between the initial velocity of hydrolysis of Ac-Pro-Phe-Arg-OMe,HCl and enzyme concentration in the range 0--150 pM. At temperatures of 30 degrees C and below substantial deviations from linearity are observed over the same enzyme concentration range. The temperature-dependent autoinhibition of kallikrein I activity is reversible and is not due to low-molecular-weight endogenous inhibitors or cofactors. The kinetic effect is apparently due to aggregation and can be abolished by the addition of sodium deoxycholate.
在37℃时,人血浆激肽释放酶I遵循米氏动力学行为,在0-150 pM范围内,Ac-Pro-Phe-Arg-OMe·HCl的水解初速度与酶浓度之间呈现正常的线性关系。在30℃及以下温度时,在相同的酶浓度范围内观察到与线性关系有显著偏差。激肽释放酶I活性的温度依赖性自抑制是可逆的,且不是由于低分子量内源性抑制剂或辅因子所致。这种动力学效应显然是由于聚集引起的,并且可以通过添加脱氧胆酸钠来消除。