DnaK ATPase activity revisited.
FEBS Lett
; 336(1): 124-8, 1993 Dec 20.
Article
em En
| MEDLINE
| ID: mdl-8262193
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Adenosina Trifosfatases
/
Proteínas de Choque Térmico HSP70
/
Proteínas de Escherichia coli
/
Proteínas de Choque Térmico
Idioma:
En
Ano de publicação:
1993
Tipo de documento:
Article