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ATPase activity of cytosolic chaperone Hsp70 from maize endosperm cell

Zhou Rengang, Miernyk J A

Institute of Agro-physics,Physiology and Biochemistry,Hebei Academy of Agricultural Sciences.Shijiazhuang 050051,Hebei

Abstract

The cytosolic chaperone Hsp70 protein from maize endosperm cell was purified. The Hsp70 have a low-level ATPase activity at normal temperature. In vitro the ATPase activity of the Hsp70 was maximal at 50℃, pH 5.8, and a KCl concentration of 20 mmol/L. It^s activity was decreased with increasing concentration of magnesium or calcium from 0 to 20 mmol/L. The co-chaperone protein from E. coli, DnaJ protein, increased the ATPase activity of maize Hsp70 about 6-fold, while GrpE, also a co-chaperone protein from E. coli, had no effect.

Key words: Heat shock protein;Molecular chaperone;ATPase activity;maize (Zea mays L.)

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Citing This Article：

Zhou Rengang, Miernyk J A. ATPase activity of cytosolic chaperone Hsp70 from maize endosperm cell. Acta Physiol Sin 1999; 51 (3): (in Chinese with English abstract).