Kinetics of fatty acid binding ability of glycated human serum albumin

Journal of biosciences

Minoru Inagaki²  Tetsuji Inoue¹  Eiji Yamazaki1¹  Osamu Kurita¹ 

[1] Industrial Research Division, Science and Technology Promotion Center, Mie Prefecture, Takachaya 5-5-45, Tsu, Mie 514-0819, Japan$$;Department of Life Sciences, Faculty of Bioresources, Mie University, Tsu, Mie, Japan$$

关键词: 1-anilino-8-naphtharene sulphonic acid;    diabetes;    dissociation constant;    fatty acids binding;    fluorescence displacement assay;    glycation;    human serum albumin.;   

DOI  :  

来源: Indian Academy of Sciences

【 摘 要 】

Kinetics of fatty acid binding ability of glycated human serum albumin (HSA) were investigated by fluorescent displacement technique with 1-anilino-8-naphtharene sulphonic acid (ANS method), and photometric detection of nonesterified-fatty-acid (NEFA method). Changing of binding affinities of glycated HSA toward oleic acid, linoleic acid, lauric acid, and caproic acid, were not observed by the ANS method. However, decreases of binding capacities after 55 days glycation were confirmed by the NEFA method in comparison to control HSA. The decrease in binding affinities was: oleic acid (84%), linoleic acid (84%), lauric acid (87%), and caproic acid (90%), respectively. The decreases were consistent with decrease of the intact lysine residues in glycated HSA. The present observation indicates that HSA promptly loses its binding ability to fatty acid as soon as the lysine residues at fatty acid binding sites are glycated.

【 授权许可】

Unknown