Zur Toxikologie von Carbromal

✍ Scribed by H. -W. Vohland; B. Streichert

• Book ID: 104735479
• Publisher: Springer-Verlag
• Year: 1978
• Tongue: English
• Weight: 458 KB
• Volume: 41
• Category: Article
• ISSN: 0340-5761
• DOI: 10.1007/bf00351771

✦ Synopsis

The binding of carbromal and its metabolites bromoethylbutyramide and ethylbutyrylurea to human plasma proteins was investigated in vitro by use of Sephadex| equilibrium dialysis and ultrafdtration. No differences appeared in the binding characteristics of human plasma and of human albumine. In a concentration range between 3 9 10 -8 and 1.5 9 10 -6 moles/ml about 40% of the carbromal, and in a concentration range between 3 9 10-: 8 and 1 9 10 -5 moles/ml about 30% of the bromoethylbutyramide are bound to plasma proteins. Proteinbinding of ethylbutyrylurea was found to be less than 5%.

The binding constants, Ka, to human albumine and the binding energies-A F ~ were found to be in the range of 0.5--1.2.103 L/Mol and 1.7--4.4 kcal/Mol, respectively.

Protein binding of carbromal, bromoethylbutyramide, their chlorinated analgous compounds, chloroethylbutyrylurea and chloroethylbutyramide, and of ethylbutyrylurea is strongly correlated to the partition coefficients of these compounds between n-octanol and water, indicating that the intensity of proteinbinding depends on the hydrophobic character of the substances tested.