Tieghem E, Van Dael H, Van Cauwelaert F
Interdisciplinair Research Centrum, Kortrijk, Belgium.
J Inorg Biochem. 1991 May 1;42(2):119-31. doi: 10.1016/0162-0134(91)80038-j.
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.
在多种条件下记录了牛α-乳白蛋白与连续的Cu(II)离子相互作用产生的可见和紫外圆二色光谱。可以根据两种结合位点对观察到的电荷转移和d-d带跃迁进行分析：分别是在组氨酸残基处和N端氨基处。在碱性pH条件下，肽主链的酰胺氮逐渐参与配位。Ca(II)和Mn(II)对高亲和力钙结合位点的占据不影响Cu(II)的结合过程，这表明该位点与Cu(II)结合位点之间没有直接相互作用。
