DNAK ATPASE ACTIVITY REVISITED

被引：44

作者：

PALLEROS, DR ^{[1
]}

REID, KL ^{[1
]}

SHI, L ^{[1
]}

FINK, AL ^{[1
]}

机构：

[1] UNIV CALIF SANTA CRUZ, DEPT CHEM & BIOCHEM, SANTA CRUZ, CA 95064 USA

来源：

FEBS LETTERS | 1993年 / 336卷 / 01期

关键词：

DNAK; HSP70; MOLECULAR CHAPERONE; ATPASE; OLIGOMER;

D O I：

10.1016/0014-5793(93)81624-9

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：

It has recently been reported that the ATPase activity of DnaK, a 70 kDa heat shock protein from E. coli, is autostimulated by increasing protein concentration [(1993) FEBS Lett. 322, 277-279], suggesting that the DnaK dimer may be the enzymatically active species. In this paper we investigated the ATPase activity of different DnaK preparations; we found that the turnover number was very dependent on protein purification. With HPLC-purified DnaK we found a turnover number 20- to 50-fold lower than typical values previously published and no evidence of autostimulation, indicating that the monomer is the active species.

引用

页码：124 / 128

页数：5

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