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首页> 外文期刊>Electroanalysis >Differential pulse polarography of the Zn2+ complexation by glutathione fragments Cys-Gly and gamma-Glu-Cys
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Differential pulse polarography of the Zn2+ complexation by glutathione fragments Cys-Gly and gamma-Glu-Cys

机译：谷胱甘肽片段Cys-Gly和γ-Glu-Cys络合Zn2 +的微分脉冲极谱法

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摘要

The metal binding properties of glutathione (GSH) and their fragments gamma-Glu-Cys and Cys-Gly are of biological and environmental interest. In this work a differential pulse polarographic study of the Zn2+/gamma-Glu-Cys and Zn2+/Cys-Gly systems was carried out for a better understanding of the results obtained in previous studies on the Zn2+-GSH system. In the case of gamma-Glu-Cys, complexation with Zn2+ was not detected. In the case of Cys-Gly, the parallel analysis, by multivariate curve resolution with alternating least squares, of data from the titration of peptide with metal and of metal with peptide suggested the presence of two types of bound Zn2+. This could be attributed to Zn2+ strongly bound to two sulfur atoms of two peptides, to form a complex of 1:2 stoichiometry, and to Zn2+ weakly bound to carboxylate and/or amino groups. [References: 26]
机译：谷胱甘肽（GSH）及其片段γ-Glu-Cys和Cys-Gly的金属结合特性具有生物学和环境意义。在这项工作中，对Zn2 + /γ-Glu-Cys和Zn2 + / Cys-Gly系统进行了差分脉冲极谱研究，以更好地了解先前在Zn2 + -GSH系统中获得的结果。在γ-Glu-Cys的情况下，未检测到与Zn2 +的络合。在Cys-Gly情况下，通过用交替最小二乘法进行多变量曲线解析的平行分析，对肽与金属的滴定和金属与肽的滴定数据表明存在两种类型的结合Zn2 +。这可能归因于Zn2 +与两个肽的两个硫原子牢固结合，形成化学计量比为1：2的复合物，而Zn2 +与羧酸盐和/或氨基弱结合。 [参考：26]

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