DnaK ATPase activity revisited.
DnaK ATPase activity revisited.
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重新审视 DnaK ATP 酶活性。
DOI：
10.1016/0014-5793(93)81624-9
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发表时间：
1993
期刊：
影响因子：
3.5
通讯作者：
Fink,AL
中科院分区：
文献类型：
--
作者：
Palleros,DR;Reid,KL;Shi,L;Fink,AL
DnaK是一种70 kDa的热休克蛋白，它的ATP酶活性弗罗姆.大肠杆菌中，通过增加蛋白质浓度来自我刺激[（1993）FEBS Lett. 322，277 - 279]，表明DnaK二聚体可能是酶活性物质。在本文中，我们研究了不同的DnaK制剂的ATP酶活性，我们发现，周转数是非常依赖于蛋白质纯化。使用HPLC纯化的DnaK，我们发现转换数比以前发表的典型值低20 - 50倍，并且没有自刺激的证据，表明单体是活性物质。
It has recently been reported that the ATPase activity of DnaK, a 70 kDa heat shock protein fromE. 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.