Three aspecific ATPases in Trichomonas vaginalis.
1. Three aspecific ATPases were found in the sedimentible fractions of Trichomonas vaginalis. 2. One, with a pH optimum of 5.5, was equally activated by Ca2+ or Mg2+, moderately stable, preferred nucleotide diphosphates as substrates, and was inhibited by vanadate, oligomycin, nitrate and Na+. 3. A second, with a pH optimum of 7.5, was activated by Mg2+, preferred guanosine diphosphate as substrate, and was the least stable and most subject to inhibitors (vanadate, oligomycin, NEM, NBD-Cl, azide and Cl-). 4. The third, pH optimum 8.0, was activated by Ca2+, was latent and the most stable, reacted equally well with nucleotide tri- or diphosphates, and was the least susceptible to inhibitors (vanadate and NEM). 5. All exhibited proton-translocating ability.
Turner
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AC
Department of Preventive Medicine, University of Mississippi Medical Center, Jackson 39216-4505.
Lushbaugh
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WB
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D002458:Cell Fractionation; D002712:Chlorides / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D013050:Spectrometry, Fluorescence; D013379:Substrate Specificity; D014246:Trichomonas vaginalis / Q000201:enzymology*
D002712:Chlorides; D000251:Adenosine Triphosphatases