Effect of temperature and chloride on steady-state inhibition of angiotensin I-converting enzyme by enalaprilat and ramiprilat.
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.
Skoglof
A
A
Department of Biochemistry and Biophysics, Chalmers University of Technology, Göteborg, Sweden.
Göthe
P O
PO
Deinum
J
J
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000494:pharmacology*; D000818:Animals; D002712:Chlorides / Q000494:pharmacology*; D015773:Enalaprilat / Q000494:pharmacology*; D007700:Kinetics; D008168:Lung / Q000201:enzymology; D008433:Mathematics; D015394:Molecular Structure; D011758:Pyrroles / Q000494:pharmacology*; D011817:Rabbits; D017257:Ramipril / Q000031:analogs & derivatives*; D012965:Sodium Chloride / Q000494:pharmacology; D013816:Thermodynamics
D000806:Angiotensin-Converting Enzyme Inhibitors; D002712:Chlorides; D011758:Pyrroles; D012965:Sodium Chloride; C052549:ramiprilat; D015773:Enalaprilat; D017257:Ramipril