High-affinity binding of warfarin, salicylate and diazepam to natural mutants of human serum albumin modified in the C-terminal end.

doi:10.1016/0006-2952(92)90466-v

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Article

High-affinity binding of warfarin, salicylate and diazepam to natural mutants of human serum albumin modified in the C-terminal end.

Biochemical pharmacology - 20 Oct 1992

Vestberg K, Galliano M, Minchiotti L, Kragh-Hansen U

Abstract excerpt

High-affinity binding of warfarin, salicylate and diazepam to four natural mutants of human serum albumin was studied by equilibrium dialysis at pH 7.4. The mutants Alb Milano Fast and Alb Vanves possess single amino acid substitutions close to the C-terminus, namely 573 Lys-->Glu and 574 Lys-->A...

Topics

Binding Sites
Diazepam
Humans
Lysine
Mutation
Protein Conformation
Salicylates
Serum Albumin
Warfarin

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