α‐Lactalbumin: structure and function

FEBS Letters

Berliner, Lawrence J.¹  Permyakov, Eugene A.² 

[1] Department of Chemistry, The Ohio State University, Columbus, OH 43210, USA;Institute for Biological Instrumentation of the Russian Academy of Sciences, 142292 Pushchino, Moscow region, Russia

关键词: α-Lactalbumin;    Structure;    Function;    Metal cation binding;    α-LA;    α-lactalbumin;    GT;    galactosyltransferase;    DMPC;    dimyristoylphosphatidylcholine;    DPPC;    dipalmitoylphosphatidylcholine;    DSA;    5-doxylstearic acid;    DSC;    differential scanning calorimetry;   

DOI  :  10.1016/S0014-5793(00)01546-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Small milk protein α-lactalbumin (α-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 α-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 α-LA demonstrate bactericidal activity and some of them cause apoptosis of tumor cells.

【 授权许可】

Unknown