FEBS Letters | |
DnaK ATPase activity revisited | |
Fink, Anthony L.1  Palleros, Daniel R.1  Shi, Li1  Reid, Katherine L.1  | |
[1] Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA | |
关键词: DnaK; hsp70; Molecular chaperone; ATPase; Oligomer; BSA; bovine serum albumin; DTT; dithiothreitol; EDTA; ethylenediaminetetraacetic acid; HMWS; high molecular weight species; HPLC; high performance liquid chromatography; hsp70; 70 kDa heat-shock proteins; PAGE; polyacrylamide gel electrophoresis; RCMLA; reduced carboxymethylated α-lactalbumin; SDS; sodium dodecyl sulfate; SEC; size exclusion chromatography; TLC; thin-layer chromatography; | |
DOI : 10.1016/0014-5793(93)81624-9 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 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.
【 授权许可】
Unknown
【 预 览 】
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RO201912020298888ZK.pdf | 636KB | download |