Isolation and Kinetic Analyses of the Soluble F1 ATPases from Mitochondria of Wheat and Pearlmillet

Aniruddha P. Sane, Vidhu A. Sane
1998 Zeitschrift für Naturforschung C - A Journal of Biosciences  
The mitochondrial F1 ATPases from two cereal crops, wheat and pearlmillet, were purified and studied. The wheat F1 ATPase could be purified to homogeneity and is apparently com­posed of six subunits with apparent molecular weights of 55 kDa (α and β), 35 kDa (γ), 26 kDa (δ') and 22 kDa (δ). The e subunit was barely detectable. Both enzymes reveal typical non-linear kinetics but show variability in their response to bicarbonate and chloride. While the wheat F1 ATPase is stimulated by bicarbonate
more » ... ated by bicarbonate and chloride, the pearlmillet F1 ATPase is inhibited by both anions. The two enzymes are Mg2+ dependent ATPases and are competitively inhibited by Ca2+, unlike maize, pea and turnip ATPases. Both the enzymes also possess a GTPase activity which is two fold higher than the ATPase, unlike rice, sorghum and oat root F1 ATPases.
doi:10.1515/znc-1998-5-607 fatcat:656gyn63lrhnbgrcw76ytad6o4