Bhaduri A, Matsudomi N, Das K P
Department of Chemistry, Bose Institute, Calcutta, India.
Biosci Biotechnol Biochem. 1996 Oct;60(10):1559-64. doi: 10.1271/bbb.60.1559.
This paper reports the effect of modification of lysine residues on the adsorption of ovalbumin at alumina/water interface. It has been shown that the pH dependence of the adsorption changes on acetylation of lysine. Thus at pH 7.6 acetylated ovalbumin does not show any affinity for alumina surface although unmodified protein does. It seems that although electrostatic interactions are operative, surface unfolding of proteins and surface hydrophobicity of protein also control the adsorption of ovalbumin onto alumina.
本文报道了赖氨酸残基修饰对卵清蛋白在氧化铝/水界面吸附的影响。结果表明，赖氨酸乙酰化后吸附的pH依赖性发生了变化。因此，在pH 7.6时，乙酰化卵清蛋白对氧化铝表面没有任何亲和力，而未修饰的蛋白质则有。虽然静电相互作用起作用，但蛋白质的表面展开和蛋白质的表面疏水性似乎也控制着卵清蛋白在氧化铝上的吸附。
