J Integr Plant Biol. ›› 1998, Vol. 40 ›› Issue (3): -.
• Research Articles •
SUN Xu-Tong, ZHOU Ren-Gang, TANG Wen-Qiang and SUN Da-Ye
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.
Maize cytosolic 70 kD stress protein,
SUN Xu-Tong, ZHOU Ren-Gang, TANG Wen-Qiang and SUN Da-Ye. Purification of Maize Cytosolic 70 kD Stress Protein: a Calmodulin-binding Protein in Plants[J]. J Integr Plant Biol., 1998, 40(3): -.
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