Adams P A, Swart E R
Biochem J. 1977 Jan 1;161(1):83-92. doi: 10.1042/bj1610083.
Precise studies were performed on the effect of temperature on the rate and equilibrium parameters characterizing the individual stages of the alpha-chymotrypsin-catalysed hydrolysis of non-specific p-nitrophenol esters at pH 7.40 and 8.50. At both pH values the results indicate that a sharp kinetic anomaly is observed in Arrhenius plots of these parameters for the binding and acylation stages of the process, but not for the deacylation stage. Detailed comparison with other kinetic studies was made, and a comparison with thermal transitions observed in alpha-chymotrypsin by using physical techniques was attempted. A detailed discussion of possible causes of the anomalies is given.
针对温度对表征α-胰凝乳蛋白酶在pH 7.40和8.50条件下催化非特异性对硝基苯酚酯水解各个阶段的速率和平衡参数的影响,进行了精确研究。在这两个pH值下,结果表明,在该过程的结合和酰化阶段,这些参数的阿仑尼乌斯图中观察到明显的动力学异常,但在脱酰化阶段未观察到。与其他动力学研究进行了详细比较,并尝试与使用物理技术在α-胰凝乳蛋白酶中观察到的热转变进行比较。对异常现象的可能原因进行了详细讨论。