Immunochemical evidence for an active (F1-F0)-ATPase in mycoplasmas.
In all Acholeplasma, Mycoplasma and Spiroplasma species tested, a protein capable of reacting with antibodies prepared against the beta subunit of the proton-ATPase complex from yeast, chloroplasts and Escherichia coli was detected. The reactive protein of M. gallisepticum was found to be catalytically active, suggesting that mycoplasmas, as other bacteria, possess a proton-translocating ATPase. Characterization of the ATPase activity of M. gallisepticum indicates that this organism also possesses a Na+-stimulated ATPase activity that differs from the proton-ATPase in its pH profile and its resistance to dicyclohexylcarbodiimide (DCCD).
D000907:Antibodies, Bacterial / Q000276:immunology; D001426:Bacterial Proteins / Q000032:analysis* / Q000037:antagonists & inhibitors / Q000276:immunology; D003429:Cross Reactions; D006863:Hydrogen-Ion Concentration; D009174:Mycoplasma / Q000201:enzymology; D009179:Mycoplasmatales / Q000201:enzymology* / Q000276:immunology; D010802:Phylogeny; D006180:Proton-Translocating ATPases / Q000032:analysis* / Q000037:antagonists & inhibitors / Q000276:immunology; D013045:Species Specificity
D000907:Antibodies, Bacterial; D001426:Bacterial Proteins; D006180:Proton-Translocating ATPases