尿毒症物質の血清蛋白結合の特性に関する研究

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  • ニョウドクショウ ブッシツ ノ ケッセイ タンパク ケツゴウ ノ トクセイ ニ カンスル ケンキュウ

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Abstract

type:P(論文)

The interaction of uremic toxins, indoxyl sulfate (IS), indoleacetic acid (IA) 3-carboxy-4-methyl-5-propyl-2-furanpropanoic acid (CMPF), with human serum albumin (HSA) was investigated by ultrafiltration and spectroscopic methods including ultra violet and fluorescence probe method. The primary binding site of IA and IS was designated site II, and the CMPF binding site was site I on the HSA molecule, as indicated by displacement experiments using different site-selective probes. Tyrosine (Tyr) and lysine (Lys) amino acid residues were probably involved in the binding sites of uremic toxins (IS, IA, CMPF) to HSA. Both hydrophobic and electrostatic interactions were found to play a role in the binding of uremic toxins to HSA. Binding of CMPF was sensitive to the N-B transition of HSA. It is suggested that the binding sites consist of a cationic site on the surface of the HSA molecule with a hydrophobic crevice to accommodate the aromatic ring of the uremic toxins. The results obtained in this study will be useful for the exact understanding of the characteristics of protein binding sites of uremic toxins.

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