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- W2034809579 abstract "The binding of the prodrug benazepril and its active metabolite benazeprilat to human serum albumin (HSA) and to human serum proteins was studied in vitro by equilibrium dialysis using 14C-labelled compounds. The extent of binding to serum proteins was high for both benazepril (94%), from 0.43 to 21.7 μmol/l and benazeprilat (93%), from 0.5 to 25.2 μmol/l. Benazepril and benazeprilat did not compete for the same site. The binding to each other was not modified in the presence of the other. Albumin was the main protein involved in the binding (77–93%). The binding of benazeprilat to HSA seemed to be decreased by the fatty acid content of HSA. The binding to HSA was characterized by two classes of sites (k1=(2.6±1.6)×104 M−1, n1=0.85±0.31 and k2=(1.0±0.7)×104 M−1, n2=7.5±4.0) for benazepril, and by one class of sites (k1=8.8×104 M−1, n1=1.2) for benazeprilat." @default.
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- W2034809579 date "1996-05-01" @default.
- W2034809579 modified "2023-09-23" @default.
- W2034809579 title "Benazepril and benazeprilat binding to albumin and serum proteins" @default.
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- W2034809579 doi "https://doi.org/10.1016/0928-0987(95)00041-0" @default.
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