BINDING OF COPPER AND ZINC IONS TO POLYPEPTIDES CONTAINING GLUTAMIC-ACID AND TYROSINE RESIDUES

被引：4

作者：

BERE, A ^{[1
]}

HELENE, C ^{[1
]}

机构：

[1] MUSEUM NATL HIST NAT, BIOPHYS LAB, F-75231 PARIS 05, FRANCE

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 1979年 / 1卷 / 05期

关键词：

D O I：

10.1016/0141-8130(79)90018-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The binding of Cu++ and Zn++ ions to three polypeptides containing Glu and Tyr residues, (Glu Tyr Glu)n, (Glu-Glu-Tyr-Glu)n and (Glu-Tyr-Tyr-Glu)n has been investigated by absorption spectroscopy, fluorescence and circular dichroism. Difference absorption spectra show that Zn+- slightly perturbs the absorption spectrum of the tyrosyl residue whereas Cu++ binding is accompanied by the appearance of a strong absorption band around 245 nm. The fluorescence of the tyrosyl residue is enhanced by Zn++ ions while it is quenched by Cu++ ions. Cation binding induces a conformational change of the polypeptides from a random coil to an α-helix, Mg++ ions do not elicit any of these phenomena. © 1979.

引用

页码：227 / 232

页数：6

共 30 条

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