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In vitro stability of the inhibition of serum converting enzyme by fosinopril
Author(s) -
Grima M.,
Barthelmebs M.,
Stephan D.,
Welsch M.,
Imbs JL
Publication year - 1992
Publication title -
fundamental and clinical pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.655
H-Index - 73
eISSN - 1472-8206
pISSN - 0767-3981
DOI - 10.1111/j.1472-8206.1992.tb00098.x
Subject(s) - fosinopril , captopril , angiotensin converting enzyme , chemistry , ace inhibitor , enzyme , in vitro , pharmacology , enzyme inhibitor , endocrinology , medicine , biochemistry , blood pressure
Summary— With captopril, it has been shown that an erroneous measurement of serum angiotensin converting enzyme (ACE) can be induced by the dissociation of the inhibitor‐ACE complex during long‐term storage. We have studied the possible dissociation of the fosinopril‐ACE complex during the storage of serum samples from healthy male volunteers given a single dose of fosinopril. Serum samples were collected from 5 volunteers, 5 min before, then 4 and 24 h after a unique oral dose of 10 mg fosinopril. ACE activity was measured by a colorimetric and a fluorimetric assay during the hour following the sampling (day 0) and after 21 or 61 days of storage at −20 or −196°C. The degree of ACE inhibition measured in vitro in fresh serum samples differed according to the technique used. Fosinopril has a long‐lasting effect with 80% inhibition 24 hours after drug administration. Storage at −20 and −196°C induced a significant decrease in the degree of inhibition measured with the colorimetric method. With the fluorimetric method, a decrease in ACE inhibition was only observed after storage at −20°C but not at −196°C.