Iwatsuru M, Nishigori H, Maruyama K
J Pharmacobiodyn. 1981 Nov;4(11):851-9. doi: 10.1248/bpb1978.4.851.
The characteristics of the binding site in the first binding class of naphthol yellow-S (NY-S) on bovine serum albumin (BSA) were studied. The binding of NY-S to BSA at an equimolar ratio of each material resulted in a marked quenching of intrinsic fluorescence of BSA and a decrease in the binding capacity of 1-anilinonaphthalene-8-sulfonate to BSA. The binding of NY-S to BSA was diminished by the chemical modification of tryptophan residue in the BSA molecule with 2-hydroxy-5-nitrobenzyl bromide and o-nitrophenylsulfenyl chloride. The higher modifications rate of tryptophan residue decreased the binding constant of NY-S to BSA. These results suggest that the first binding site of NY-S to BSA is located in a hydrophobic area including tryptophan which is position 134 on the amino acid sequence of BSA. Studies on BSA modified with diethylpyrocarbonate demonstrated that a histidine residue also may participate in the binding of NY-S to BSA.
研究了萘酚黄-S（NY-S）在牛血清白蛋白（BSA）上第一结合类别的结合位点特征。以等摩尔比的每种物质使NY-S与BSA结合，导致BSA的固有荧光显著猝灭，且1-苯胺基萘-8-磺酸盐与BSA的结合能力降低。用2-羟基-5-硝基苄基溴和邻硝基苯亚磺酰氯对BSA分子中的色氨酸残基进行化学修饰，会减少NY-S与BSA的结合。色氨酸残基的修饰率越高，NY-S与BSA的结合常数越低。这些结果表明，NY-S与BSA的第一个结合位点位于包括色氨酸的疏水区域，色氨酸在BSA氨基酸序列中位于第134位。对用焦碳酸二乙酯修饰的BSA的研究表明，组氨酸残基也可能参与NY-S与BSA的结合。
