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Molecular Pharmacology, Vol 15, 754-757, Copyright © 1979 by the American Society for Pharmacology and Experimental Therapeutics

Characterization of a Specific Drug Binding Site of Human Serum Albumin

NICHOLAS P. SOLLENNE 1 and GARY E. MEANS 1

1 Department of Biochemistry, The Ohio State University, 484 W. 12th Avenue, Columbus, Ohio 43210

The rapid reaction of p-nitrophenyl acetate with human serum albumin is stoichiometrically inhibited by the binding of ligands in a specific apolar anion binding site. Inhibition of the reaction by certain ligands, incbuding many drugs, thus affords a convenient and sensitive means to detect and study their interactions with that site. Procedures for the general qualitative and quantitative characterization of interactions of ligands with the p-nitrophenyl acetate reactive site are described and preliminary results obtained with six well known drugs are presented.

Note:
ACKNOWLEDGMENTS We want to thank S. W. Margaret Koh for her assistance and discussions which made thin work possible and Hoffmann LaRoche Inc., The Upjohn Co. and Syntex Laboratories Inc. for their gifts of chlordiazepoxide, ibuprofen, and naproxen, respectively.

Submitted on June 12, 1978
Accepted on October 31, 1978




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