A CIRCULAR DICHROIC STUDY OF CU(II) BINDING TO BOVINE ALPHA-LACTALBUMIN

被引：11

作者：

TIEGHEM, E ^{[1
]}

VANDAEL, H ^{[1
]}

VANCAUWELAERT, F ^{[1
]}

机构：

[1] KATHOLIEKE UNIV LEUVEN,INTERDISCIPLINAIR RES CENTRUM,UNIV CAMPUS,B-8500 KORTRIJK,BELGIUM

来源：

JOURNAL OF INORGANIC BIOCHEMISTRY | 1991年 / 42卷 / 02期

关键词：

D O I：

10.1016/0162-0134(91)80038-J

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 visible and ultraviolet circular dichroic spectra resulting from the interaction of bovine alpha-lactalbumin with successive Cu(II) ions have been recorded under a variety of conditions. Analysis of the observed charge-transfer and d-d band transitions can be made in terms of two kinds of binding sites: at a histidyl group and at the N-terminal amino group, respectively. At basic pH the amide nitrogens of the peptide backbone progressively take part in the coordination. The occupation of the high affinity calcium binding site by Ca(II) and Mn(II) does not influence the Cu(II) binding process, suggesting that there is no direct interaction between this site and the Cu(II) binding sites.

引用

页码：119 / 131

页数：13

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