A circular dichroic study of Cu(II) binding to bovine alpha-lactalbumin.

Abstract:

: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 change-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.

journal_name

J Inorg Biochem

authors

Tieghem E,Van Dael H,Van Cauwelaert F

doi

10.1016/0162-0134(91)80038-j

subject

Has Abstract

pub_date

1991-05-01 00:00:00

pages

119-31

issue

2

eissn

0162-0134

issn

1873-3344

pii

0162-0134(91)80038-J

journal_volume

42

pub_type

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