Evaluation of hydrophobicity versus chaperonelike activity of bovine αA- and αB-Crystallin

被引：23

作者：

Bhattacharyya, J

Srinivas, V

Sharma, KK ^{[1
]}

机构：

[1] Univ Missouri, Dept Ophthalmol, Columbia, MO 65212 USA

[2] Univ Missouri, Dept Biochem, Columbia, MO 65212 USA

来源：

JOURNAL OF PROTEIN CHEMISTRY | 2002年 / 21卷 / 01期

关键词：

alpha A-crystallin; alpha B-crystallin; hydrophobicity;

D O I：

10.1023/A:1014187300930

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：

Calf lens alphaA-crystallin isolated by reversed-phase HPLC demonstrates a slightly more hydrophobic profile than alphaB-crystallin. Fluorescent probes in addition to bis-ANS, like cis-parinaric acid (PA) and pyrene, show higher quantum yields or Ham ratios when bound to alphaA-crystallin than to alphaB-crystallin at room temperature. Bis-ANS binding to both alphaA- and alphaB-crystallin decreases with increase in temperature. At room temperature, the chaperone-like activity of alphaA-crystallin is lower than that of alphaB-crystallin whereas at higher temperatures, alphaA-crystallin shows significantly higher protection against aggregation of substrate proteins compared to alphaB-crystallin. Therefore, calf lens alphaA-crystallin is more hydrophobic than alphaB-crystallin and chaperone-like activity of alpha-crystallin subunits is not quantitatively related to their hydrophobicity.

引用

页码：65 / 71

页数：7

共 48 条

[1] The structural differences between bovine lens αA- and αB-crystallin [J].