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- W1988351852 abstract "Abstract The binding of cefotiam and cyclohexanol to human serum, isolated proteins and erythrocytes has been studied in-vitro by equilibrium dialysis. The two molecules are 50% bound to serum proteins and the free fraction for both compounds remained constant within the therapeutic concentration range. Human serum albumin (HSA) was exclusively responsible for the cefotiam binding (48%) with a saturable process characterized by one binding site (n=1·00±0·14) with a very weak affinity (Ka=1457 ± 352 m−1). Like other cephalosporins, cefotiam showed no binding to α1-acid glycoprotein, lipoproteins or γ-globulins. Cyclohexanol is mainly bound to HSA with a weak affinity (Ka ∼ 1 800 m−1) but lipoproteins and α1-acid glycoprotein bind about 30% of bound cyclohexanol in serum. Interactions with free fatty acids (FFA) or bilirubin were studied at physiopathological concentrations. HSA-bound cefotiam was displaced by FFA (1260 μM) and bilirubin (330 μM), whereas the cyclohexanol binding was inhibited only by FFA. The cefotiam binding site seems to be close to the warfarin site (site I) whereas cyclohexanol probably shares the diazepam site (site II) on HSA. There is no mutual inhibition of binding between cefotiam and cyclohexanol at therapeutic levels. The binding of both compounds to erythrocytes is low and restricted when measured in the presence of plasma." @default.
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- W1988351852 date "1991-12-01" @default.
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- W1988351852 title "The blood binding of cefotiam and cyclohexanol, metabolites of the prodrug cefotiam hexetil, in-vitro" @default.
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- W1988351852 doi "https://doi.org/10.1111/j.2042-7158.1991.tb03196.x" @default.
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