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血清白蛋白是血清中含量最丰富的蛋白质,是多种金属离子的输运蛋白。钴(Ⅱ)离子在金属蛋白研究中经常被用作光谱探针。但Co(Ⅱ)与血清白蛋白的相互作用却很少被研究。50年代Rao和Lal用光谱和电泳法推断,Co(Ⅱ)与BSA(Bovine serum albumin,牛血清白蛋白)的结合仅有羧基参与,但他们未能解释为何含氮基团完全不参与配位。本文利用紫外光谱发现在生理pH条件下,钴离子与HSA(Human serum albumin,人血清白蛋白)和BSA的1:1配合物可能有包含羧基和α-NH_2基的混合配位环境,取六配位的八面体构型,金属离子以Co(Ⅱ)和Co(Ⅲ)两种氧化态存在。
Serum albumin is the most abundant serum protein, is a variety of metal ion transport protein. Cobalt (II) ions are often used as spectral probes in metalloprotein studies. However, the interaction between Co (II) and serum albumin is seldom studied. In the 1950s, Rao and Lal used spectroscopy and electrophoresis to infer that the binding of Co (Ⅱ) to BSA (Bovine serum albumin) only involved the carboxyl group, but they failed to explain why the nitrogen-containing groups did not participate in the coordination at all . In this paper, it was found that the 1: 1 complex of cobalt ion with HSA (Human serum albumin) and BSA could have mixed coordination environment containing carboxyl group and α-NH 2 group under physiological pH conditions by using ultraviolet spectrum. Coordination octahedral configuration, the metal ions to Co (Ⅱ) and Co (Ⅲ) two oxidation states exist.