J Integr Plant Biol. ›› 1998, Vol. 40 ›› Issue (3): -.

• Research Articles •    

Purification of Maize Cytosolic 70 kD Stress Protein: a Calmodulin-binding Protein in Plants

SUN Xu-Tong, ZHOU Ren-Gang, TANG Wen-Qiang and SUN Da-Ye   

Abstract: The maize cytosolic 70 kD stress protein (HSC70) has been purified by a two-step procedure employing affinity chromatography on ATP-agarose followed by DEAE52 ion-exchange chromatography. Using a biotinylated cauliflower calmodulin (CAM) gel-overlay technique in the presence of 1 mmol/L Ca2+ , the HSCT0 could bind to CAM. No band was shown on sodium dodecyl sulfate-polyacrylamide gel overlayed with biotinylated cauliflower CaM when 1 mmoL/L Ca2+ was replaced by 5 mmol/L EGTA. It indicated that the binding of HSC70 to CaM was dependent on Ca2+. The purified HSC70 inhibited the activity of CaM-dependent NADK and the degree of inhibition increased with augmentation of the HSC70, which appeared to be typically characteristic to CaM- binding protein.

Key words: Maize cytosolic 70 kD stress protein, Calmodulin-binding protein

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