Kinetics of fatty acid binding ability of glycated human serum albumin.

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Yamazaki E, Inagaki M, Kurita O, Inoue T

Kinetics of fatty acid binding ability of glycated human serum albumin.

J Biosci. 2005 Sep;30(4):475-81.

PubMed ID

16184009 [ View in PubMed

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Abstract

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 bind-ing 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.

DrugBank Data that Cites this Article

Drug Carriers

Drug	Carrier	Kind	Organism	Pharmacological Action	Actions
Lauric acid	Serum albumin	Protein	Humans	Unknown	Not Available	Details