Binding of the organophosphates parathion and paraoxon to bovine and human serum albumin
| Autor: | J. Mourik, L. P. A. de Jong |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
Health
Toxicology and Mutagenesis Plasma protein binding Toxicology Paraoxon chemistry.chemical_compound medicine Animals Humans Binding site Bovine serum albumin Serum Albumin Binding Sites Chromatography Parathion biology Chemistry Organophosphate Albumin Serum Albumin Bovine General Medicine Human serum albumin Kinetics biology.protein Cattle Dialysis Protein Binding medicine.drug |
| Zdroj: | Archives of Toxicology. 41:43-48 |
| ISSN: | 1432-0738 0340-5761 |
| DOI: | 10.1007/bf00351768 |
| Popis: | Binding of parathion and paraoxon to bovine serum albumin (BSA) and human serum albumin (HSA) was studied by using equilibrium dialysis. The concentration of unbound organophosphate was determined from its anticholinesterase activity. Binding of parathion to BSA was shown to be reversible. The organophosphates interact with only one type of binding sites in BSA and HSA. The affinity constants at pH 7.2 and 4 degrees C for the interaction of BSA or HSA and parathion were found to be 2.7 X 10(6) and 1.5 X 10(6) M-1, respectively. The affinity constants for the interaction of the serum albumins and paraoxon were considerably lower, 6.0 X 10(3) and 1.6 X 10(4) M-1, respectively. Lowering the pH from 7.2 to 4.8 did not significantly affect the binding parameters. The great difference of affinity of the serum albumins to parathion and paraoxon is discussed with respect to the fate of parathion in the body. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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