Kinetics of fatty acid binding ability of glycated human serum albumin.
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.
Yamazaki
Eiji
E
Industrial Research Division, Science and Technology Promotion Center,Mie Prefecture, Takachaya 5-5-45, Tsu, Mie 514-0819, Japan. yamaze00@pref.mie.jp
Inagaki
Minoru
M
Kurita
Osamu
O
Inoue
Tetsuji
T
D000596:Amino Acids / Q000235:genetics; D005227:Fatty Acids / Q000378:metabolism*; D005947:Glucose / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D007700:Kinetics; D019301:Oleic Acid / Q000378:metabolism; D020539:Sequence Analysis, Protein; D012709:Serum Albumin / Q000235:genetics / Q000378:metabolism*
D000596:Amino Acids; D005227:Fatty Acids; D012709:Serum Albumin; D019301:Oleic Acid; D005947:Glucose