牛血清白蛋白与棉酚相互作用的化学计量分析：荧光猝灭研究。
A stoichiometric analysis of bovine serum albumin-gossypol interactions: a fluorescence quenching study.
作者信息
Rao A G
机构信息
Food Chemistry Department, Central Food Technological Research Institute, Mysore.
出版信息
Indian J Biochem Biophys. 1992 Apr;29(2):179-82.
The interaction of gossypol with bovine serum albumin, human serum albumin and n-bromosuccinimide-modified bovine serum albumin has been followed by fluorescence quenching measurements. The presence of a high affinity site (association constant K = 2.2 x 10(6) M-1) for gossypol on bovine serum albumin and human serum albumin is indicated. The stoichiometry of binding for the high affinity site was evaluated using Job's method of continuous variation, thereby suggesting the formation of 1:1 complex. Modification of the tryptophan residues on bovine serum albumin does not affect the binding of gossypol to either high or low affinity site of albumin.
通过荧光猝灭测量研究了棉酚与牛血清白蛋白、人血清白蛋白以及N-溴代琥珀酰亚胺修饰的牛血清白蛋白之间的相互作用。结果表明，棉酚在牛血清白蛋白和人血清白蛋白上存在一个高亲和力位点（缔合常数K = 2.2×10⁶ M⁻¹）。使用乔布连续变化法评估了高亲和力位点的结合化学计量，结果表明形成了1:1复合物。对牛血清白蛋白上色氨酸残基的修饰并不影响棉酚与白蛋白高亲和力或低亲和力位点的结合。
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