Site-directed mutagenesis studies of human serum albumin define tryptophan at amino acid position 214 as the principal site for nitrosation.

The patterns of nitric oxide (NO) release from nitrosated bovine serum albumin (BSA), human serum albumin (HSA) and a number of recombinant HSA mutants were compared. All albumin species were nitrosated by incubation with acidified NO(2)(-). The pattern of NO release from BSA nitrosated with acidified NO(2)(-) was in agreement with previous reports which indicated that Cys-34 is the primary target for nitrosation in BSA.

Expression of a human serum albumin fragment (consisting of subdomains IA, IB, and IIA) and a study of its properties.

Site-directed mutagenesis and a yeast expression system were used to synthesize a human serum albumin (HSA) fragment (amino acids 1-297). The HSA fragment (half HSA) was evaluated with a number of biophysical techniques and found to be similar to the corresponding region in wild-type HSA. Specifically, the circular dichroism spectra of half HSA and wild-type HSA were superimposable, indicating that the highly alpha-helical secondary structure of wild-type HSA is preserved in half HSA.

A dynamic model for bilirubin binding to human serum albumin.

Site-directed mutagenesis of human serum albumin was used to study the role of various amino acid residues in bilirubin binding. A comparison of thermodynamic, proteolytic, and x-ray crystallographic data from previous studies allowed a small number of amino acid residues in subdomain 2A to be selected as targets for substitution. The following recombinant human serum albumin species were synthesized in the yeast species Pichia pastoris: K195M, K199M, F211V, W214L, R218M, R222M, H242V, R257M, and wild type human serum albumin.

Investigations of the effects of ethanol on warfarin binding to human serum albumin.

Ethanol effects on warfarin binding to human serum albumin (HSA) have been studied by equilibrium dialysis and fluorescence methods at pH 7.4 in phosphate-buffered saline at 37 degrees C. In the presence of various amounts of ethanol fluorescence intensity of bound warfarin decreased significantly but this intensity reduction was not solely from displacement of bound warfarin from HSA.

Familial dysalbuminemic byperthyroxinemia may result in altered warfarin pharmacokinetics.

Two distinct genotypes that result in the amino acid substitutions R218P and R218H in subdomain 2A of human serum albumin (HSA) have been identified as the cause of familial dysalbuminemic hyperthyroxinemia (FDH). These substitutions increase the affinity of subdomain 2A for thyroxine by approximately 10-fold elevating plasma thyroxine levels in affected individuals. While many studies have examined the binding of thyroxine to FDH HSA, the binding of FDH HSA to drugs has not been widely investigated.