α-Lactalbumin:: structure and function

被引:418
作者
Permyakov, EA [1 ]
Berliner, LJ
机构
[1] Russian Acad Sci, Inst Biol Instrumentat, Pushchino 142292, Moscow Region, Russia
[2] Ohio State Univ, Dept Chem, Columbus, OH 43210 USA
关键词
alpha-lactalbumin; structure; function; metal cation binding;
D O I
10.1016/S0014-5793(00)01546-5
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
Small milk protein alpha-lactalbumin (alpha-LA), a component of lactose synthase, is a simple model Ca2+ binding protein, which does not belong to the EF-hand proteins, and a classical example of molten globule state, It has a strong Ca2+ binding site, which binds Mg2+, Mn2+, Na+, and K+, and several distinct Zn2+ binding sites. The binding of cations to the Ca2+ site increases protein stability against action of heat and various denaturing agents, while the binding of Zn2+ to the Ca2+-loaded protein decreases its stability. Functioning of alpha-LA requires its interactions with membranes, proteins, peptides and low molecular weight substrates and products. It was shown that these interactions are modulated by the binding of metal cations. Recently it was found that some folding variants of alpha-LA demonstrate bactericidal activity and some of them cause apoptosis of tumor cells. (C) 2000 Federation of European Biochemical Societies.
引用
收藏
页码:269 / 274
页数:6
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