Calcium-activated adenosine triphosphatase activity of pellicles from Paramecium caudatum.
Pellicles were isolated from Paramecium caudatum for a study of the properties of its insoluble ATPase [EC 3.6.1.3] activity. Pellicular ATPase was solubilized by sonication and fractionated by sucrose density gradient centrifugation. The sedimentation coefficient of the ATPase was about 9S. The ATPase required Ca2+ for maximum activation. Addition of neutral salts to the assay medium inhibited the activity. Substrate specificity for ATP was low; other nucleoside triphosphates were hydrolyzed at about the same rate as ATP; AMP, pyrophosphate, and p-nitrophenyl phosphate were not hydrolyzed. The ATPase activity of the pellicle preparation had a pH optimum at pH 6.5, and a Michaelis constant of 9 micrometer. On the other hand, the enzymatic properties of the ATPase were somewhat modified by the procedure of solubilization and fractionation. The pellicular ATPase does not resemble ciliary dynein ATPase or the soluble ATPase of Tetrahymena.
D000818:Animals; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D002413:Cations, Divalent; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010247:Paramecium / Q000201:enzymology*; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity
D002413:Cations, Divalent; D000252:Calcium-Transporting ATPases