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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    European journal of clinical pharmacology 8 (1975), S. 445-453 
    ISSN: 1432-1041
    Keywords: Amobarbital ; pentobarbital ; diphenylhydantoin ; protein binding ; erythrocytes ; uraemia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary By equilibrium dialysis of human plasma it has been shown that the binding of pentobarbital and diphenylhydantoin to plasma proteins is decreased in uraemic patients (46 and 74 per cent bound, respectively) compared to healthy volunteers (61 and 88 per cent bound). The degree of binding of pentobarbital was significantly correlated with that of diphenylhydantoin and amobarbital, which suggests similarity of their binding sites. Appreciable proportions of the drugs were found in blood cells both in healthy and uraemic subjects. As expected, the distribution of drugs in whole blood was different in the uraemics from healthy subjects, because of the decreased plasma protein binding and the lowered red cell count in uraemia. Analysis of the data showed that the ratio between the concentrations in blood cells and plasma water in uraemic patients was not significantly different from that in healthy subjects.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1041
    Keywords: Pentobarbital ; diphenylhydantoin ; salicyclic acid ; protein binding ; erythrocytes ; cell equilibration ; temperature effect
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary The binding of pentobarbital, diphenylhydantoin and salicylic acid to cells in blood was found to be independent of total drug concentration within therapeutic levels. Salicylic acid displaced pentobarbital and diphenylhydantoin from plasma protein binding sites, but high levels of salicylic acid had no effect on the distribution of the other two drugs to washed blood cells. Thus, in whole blood the presence of salicylic acid decreased the fraction of pentobarbital or diphenylhydantoin bound to plasma protiens and increased the fraction of the drug in plasma water and in blood cells. Diphenylhydantoin was shown not to be bound irreversibly to blood cells and equilibration in between the inside and outside of the cells was found to be rapid (within 5 min), even at high concentrations. Binding to washed blood cells was the same at 37°C and 25°C, in contrast to plasma protein binding. It is pointed out that these effects may cause certain analytical errors, resulting in changes in plasma concentration if plasma is separated at a low temperature.
    Type of Medium: Electronic Resource
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