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

来源：

RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY | 2012年 / 38卷 / 02期

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

页码：192 / 197

页数：6

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