N-bromosuccinimide-oxidized human serum albumin as a tool for the determination of drug binding sites of human serum albumin.
- 1 January 1983
- journal article
- research article
- Published by Pharmaceutical Society of Japan in CHEMICAL & PHARMACEUTICAL BULLETIN
- Vol. 31 (3) , 971-978
- https://doi.org/10.1248/cpb.31.971
Abstract
In order to investigate the role of the Trp residue of human serum albumin (HSA) in drug binding, HSA oxidized with 8 mol equivalents of N-bromosuccinimide (NBS) was prepared at pH 4.1. The NBS-oxidized HSA lost the lone Trp residue without change in Tyr content, and the modified protein retained the gross polypeptide conformation of native HSA as far as could be judged from the circular dichroism (CD) spectrum. The binding ability of NBS-oxidized HSA for chlordiazepoxide was decreased by about 60% from that of HSA. The binding of phenylbutazone and warfarin at the most reactive site of the modified HSA was not very different from that to HSA. The lone Trp residue in HSA apparently lies in or near the indole and benzodiazepine binding site and not in the primary binding site of warfarin and phenylbutazone.This publication has 1 reference indexed in Scilit:
- Removal of Fatty Acids from Serum Albumin by Charcoal TreatmentJournal of Biological Chemistry, 1967