Chaperone-like activity of β-casein

被引:81
作者
Zhang, XF
Fu, XM
Zhang, H
Liu, C
Jiao, WW
Chang, ZY
机构
[1] Tsinghua Univ, Dept Biol Sci & Biotechnol, Beijing 100084, Peoples R China
[2] Peking Univ, State Key Lab Prot Engn & Plant Genet Engn, Beijing 100871, Peoples R China
[3] Peking Univ, Coll Life Sci, Beijing 100871, Peoples R China
基金
中国国家自然科学基金;
关键词
beta-casein; chaperone; protein aggregation; hydrophobic;
D O I
10.1016/j.biocel.2004.12.004
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
The caseins are major components of milk for most mammals and are secreted as large colloidal aggregates termed micelles. They have less ordered secondary and tertiary structures in comparison with typical globular proteins. In this work, beta-casein, a member of the casein family, has been demonstrated to exhibit chaperone-like activity, being able to suppress the thermal and chemical aggregation of such substrate proteins as insulin, lysozyme, alcohol dehydrogenase, and catalase by forming stable complexes with the denaturing substrate proteins. Meanwhile, beta-casein was found to not only prevent aggregation of the substrate proteins, but also solubilize the protein aggregates already formed. Data also show that P-casein exhibits a higher chaperone-like activity than a-casein, likely due to the difference in the number of proline residues present and/or in the extent of exposed hydrophobic surfaces. The implications for their in vivo functions of the caseins, based on their exhibiting such in vitro chaperone-like activities, are discussed. (c) 2004 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1232 / 1240
页数:9
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