Vajda T, Garai A
J Inorg Biochem. 1981 Dec;15(4):307-15. doi: 10.1016/s0162-0134(00)80234-2.
The effect of Mn2+ and Ca2+ ions on the rate of trypsin autolysis was studied at pH 7.0 and at 34.4-60.2 degrees C. For comparison, the kinetic constants of esterolytic activity of trypsin in the presence of the metal ion were determined at pH 7.4 and at 36 degrees and 40 degrees C. There was no significant difference in the rate of autolysis between Mn2+ and Ca2+ in the temperature range 34-47 degrees C, but at 56.8 degrees and 60.2 degrees autolysis was slightly more rapid in the presence of Mn2+. The Mn2+ or Ca2+ ion bound to trypsin is supposed to control the conformation and thereby the stability and the activity of the enzyme. The indirect effect of Mn2+ and Ca2+ is discussed on a structural basis of the enzyme molecule.
在pH 7.0以及34.4 - 60.2摄氏度的条件下，研究了Mn2+和Ca2+离子对胰蛋白酶自溶速率的影响。作为对比，在pH 7.4以及36摄氏度和40摄氏度的条件下，测定了金属离子存在时胰蛋白酶酯解活性的动力学常数。在34 - 47摄氏度的温度范围内，Mn2+和Ca2+存在时的自溶速率没有显著差异，但在56.8摄氏度和60.2摄氏度时，Mn2+存在时自溶稍微快一些。与胰蛋白酶结合的Mn2+或Ca2+离子被认为可控制酶的构象，进而控制酶的稳定性和活性。基于酶分子的结构基础，讨论了Mn2+和Ca2+的间接作用。
