Angiotensin-converting enzyme inhibitors binding

ACE-I angiotensin-converting enzyme inhibitor CBG cortisol binding globulin... 

Sramko M, Garaj V, Remko M (2008) Thermodynamics of binding of angiotensin-converting enzyme inhibitors to enzyme active site model, J Mol Struct—Theochem 869(1-3) 19-28. 10.1016/j. theochem.2008.08.018... 

The Zn11 ion of angiotensin-converting enzyme (ACE) has been replaced by Co11 to give an active, chromophoric enzyme and inhibitor binding has been identified spectroscopically. Visible and MCD spectroscopy were used to characterize the catalytic metal binding site in the... 

Cheung HS, Wang EL, Ondetti MA, Sabo EF, Cushman DW. (1980) Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence. J Biol Chem 255 401-407. 

Fig. 1. The proposed binding of substrates and inhibitors to the active sites of car-boxypeptidase A and angiotensin-converting enzyme. Reproduced with permission from Ondetti et al. (95). Copyright 1977 American Association for the Advancement of Science.

Wade et al. reported the use of a novel statistical approach for the comparison of analytical methods to measure angiotensin converting enzyme [peptidyl-dipeptidase A] activity, and to measure enalaprilat and benazeprilat [8]. Two methods were used to measure peptidyl-dipeptidase A, namely hippuryl histidyl leucine (HHL-method) [9], and inhibitor binding assay (IBA method) [10]. Three methods were used to measure enalaprilat, namely a radioimmunoassay (RIA) method [11], the HHL method, and the IBA method. Three methods were used to measure benazeprilat (then active metabolite of benazepril) in human plasma, namely gas chromatography-mass spectrometry (GC-MS method) [12], the HHL method, and the IBA method, and were statistically compared. First, the methods were compared by the paired t test or analysis of variance, depending on whether two or three different methods were under comparison. Secondly, the squared coefficients of variation of the... 

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