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Isolation of peptides from uremic plasma that inhibit phenytoin binding to normal plasma proteins
Author(s) -
Kinniburgh David W,
Boyd Nigel D
Publication year - 1981
Publication title -
clinical pharmacology and therapeutics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.941
H-Index - 188
eISSN - 1532-6535
pISSN - 0009-9236
DOI - 10.1038/clpt.1981.159
Subject(s) - phenytoin , chemistry , plasma protein binding , pharmacology , blood proteins , non competitive inhibition , binding site , biochemistry , medicine , enzyme , psychiatry , epilepsy
The binding of many drugs to plasma proteins is altered in renal disease. Explanations include hypoproteinemia, alterations in the native structure of the binding protein, and competitive or noncompetitive inhibition. The binding of phenytoin to proteins was studied in plasma from patients with chronic renal failure by equilibrium dialysis at 37°. Charcoal adsorption was used to normalize the binding. Substances that appeared to be peptides were isolated; they inhibited the binding of phenytoin to normal plasma proteins. The data suggest that the defect in phenytoin‐protein binding in chronic renal failure may be due to competitive or noncompetitive inhibition by peptides. Clinical Pharmacology and Therapeutics (1981) 30, 276–280; doi: 10.1038/clpt.1981.159