Skoglof A, Göthe P O, Deinum J
Department of Biochemistry and Biophysics, Chalmers University of Technology, Göteborg, Sweden.
Biochem J. 1990 Dec 1;272(2):415-9. doi: 10.1042/bj2720415.
The kinetics of the steady-state inhibition of angiotension I-converting enzyme (EC 3.4.15.1) at 25 degrees C and 37 degrees C with enalaprilat and ramiprilat can be simulated, assuming only one inhibitor-binding site, consistent with a 1:1 stoichiometry if the protein concentration was determined by amino acid analysis. In this temperature range the apparent inhibition constants for ramiprilat and enalaprilat were roughly doubled by a decrease in the chloride concentration from 0.300 M to 0.120 M.
假设只有一个抑制剂结合位点,在25摄氏度和37摄氏度下,依那普利拉和雷米普利拉对血管紧张素I转换酶(EC 3.4.15.1)稳态抑制的动力学可以被模拟,如果通过氨基酸分析确定蛋白质浓度,则符合1:1化学计量比。在这个温度范围内,当氯化物浓度从0.300 M降至0.120 M时,雷米普利拉和依那普利拉的表观抑制常数大约会加倍。