[Mg, Ca-activated ATP-ase of Pacinian corpuscles].
Adenosine triphosphatase (ATPase) activated by Mg2+ or Ca2+ ions was detected in single mechanoreceptors (Pacini's corpuscles) of cat; addition of Ca2+ (10(-5)M) to Mg-ATP-ase increased the activity by the factor of 1.6. The activity optimum of Mg- or Co-ATPase was in the alkaline pH zone. A high substrate specificity of Mg, Ca-ATPase was shown. Parachlorinemercury-benzoate (5muM) considerably reduced the activity of Mg, Ca-ATPase, whereas oubain (10(-5)M) failed to affect it significantly. It is supposed that Mg, Ca-ATPase of Pacini's corpuscles was close to actomyosine -like proteins.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D002118:Calcium; D002384:Catalysis; D002415:Cats; D002729:Chloromercuribenzoates; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007700:Kinetics; D008274:Magnesium; D008465:Mechanoreceptors / Q000201:enzymology*; D010042:Ouabain; D010141:Pacinian Corpuscles / Q000201:enzymology*
D002729:Chloromercuribenzoates; D010042:Ouabain; D000251:Adenosine Triphosphatases; D008274:Magnesium; D002118:Calcium
Mg, Ca-aktiviruemaia ATF-aza telets Pachini