Abstract
Abstract
The appropriate conditions for determining angiotensin-converting enzyme in human serum with use of 2-furanacryloyl-L-phenylalanylglycylglycine as substrate are described. The method, a modification of that reported by Holmquist et al. (Anal. Biochem. 95:540-548, 1979) for purified rabbit lung enzyme, is based on the blue shift of the absorption spectrum that occurs upon hydrolysis of the substrate into furanacryloyl-L-phenylalanine and glycylglycine. The Km value for the substrate is 0.31 mmol/L. Some kinetic properties determined by this method are similar to those previously reported for the purified serum enzyme. Results by the present assay and Cushman's modified method correlate closely (r = 0.995). The normal reference interval for 42 adult donors was 43-137 U/L (mean 90 U/L, SD 23 U/L). The within-run and between-run CVs ranged from 3.0 to 4.1%. Its rapidity, simplicity, sensitivity, and precision make the proposed method very suitable for routine work, clinical investigation, and kinetic and structural studies of the serum enzyme.
Publisher
Oxford University Press (OUP)
Subject
Biochemistry (medical),Clinical Biochemistry
Cited by
55 articles.
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