胆红素与配体蛋白及氨基偶氮染料结合蛋白A结合的光谱学研究。
Spectroscopic studies of the binding of bilirubin by ligandin and aminoazo-dye-binding protein A.
作者信息
Tipping E, Ketterer B, Christodoulides L, Enderby G
出版信息
Biochem J. 1976 Jul 1;157(1):211-6. doi: 10.1042/bj1570211.
Abstract
Ligandin and aminoazo-dye-binding protein A both bind bilirubin at a single site. Quantitative studies of the interactions using difference spectrophotometry show that at pH 7.0, protein A binds the tetrapyrrole with an association constant (K) greater than or equal to 2 X 10(7) litre/mol, whereas binding by ligandin is slightly weaker (K = 7 X 10(6) litre/mol) at this pH. The protein-bilirubin complexes give rise to absorption and fluorescence spectra quite different from those of unbound bilirubin and also to large Cotton effects. It appears that on binding to both proteins, the ligand is forced into a rigid twisted configuration in a hydrophobic environment. Ligandin and protein A resemble serum albumin in their interactions with bilirubin.
摘要
配体结合蛋白和氨基偶氮染料结合蛋白A均在单一位点结合胆红素。使用差示分光光度法对相互作用进行的定量研究表明，在pH 7.0时，蛋白A与四吡咯结合的缔合常数（K）大于或等于2×10⁷升/摩尔，而在此pH下，配体结合蛋白的结合稍弱（K = 7×10⁶升/摩尔）。蛋白质 - 胆红素复合物产生的吸收光谱和荧光光谱与未结合胆红素的光谱有很大不同，并且还产生大的科顿效应。看来，在与这两种蛋白质结合时，配体在疏水环境中被迫形成刚性扭曲构型。配体结合蛋白和蛋白A在与胆红素的相互作用方面类似于血清白蛋白。
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