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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 bicarbonatedoi:10.1515/znc-1998-5-607 fatcat:656gyn63lrhnbgrcw76ytad6o4