Chaperone-Like Activity of β-Casein and Thermal Stability of Alcohol Dehydrogenase

被引:4
作者
Zakharchenko, N. L. [1 ]
Konnova, T. A. [1 ]
Gogoleva, N. E. [1 ]
Faizullin, D. A. [1 ]
Haertle, T. [2 ]
Zuev, Yu. F. [1 ]
机构
[1] Russian Acad Sci, Kazan Sci Ctr, Kazan Inst Biochem & Biophys, Kazan 420111, Russia
[2] Inst Natl Rech Agronom Nantes, F-44316 Nantes, France
关键词
beta-casein; mutant forms; physico-chemical properties; chaperon-like activity; PROTEIN SECONDARY STRUCTURE;
D O I
10.1134/S1068162012020136
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
Correlation between structural peculiarities of beta-casein and its chaperon-like activity was investigated using the recombinant forms of the protein containing the cysteine residues in the polypeptide chain. Aggregation of native and modified forms of beta-casein was studied, as well as their chaperon-like activity towards alcohol dehydrogenase thermal aggregation. It has been shown that dimeric and oligomeric forms of beta-casein, which are formed due to intermolecular disulfide bonds, significantly differ in their physico-chemical and chaperon-like properties from monomeric forms. The thermal stability of alcohol dehydrogenase has been found to depend on the beta-casein concentration.
引用
收藏
页码:192 / 197
页数:6
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