[Alkaline phosphomonohydrolases of Pacinian corpuscles].
Research on quantitative determination of activity of alkaline phosphatase (EC) 3.1.3.1) and 5'-nucleotidase (EC 3.1.3.5) of Pacinian corpuscles was performed. Two enzymes are shown to be different, which are distinguished by the pH optimum and substrate concentration. Alkaline phosphatase is found to be more active in splitting glycerophosphates. The alkaline phosphatase activity towards beta-glycerophosphate and alpha-naphthylphosphate is caused by various enzyme molecular forms with different electrophoretic mobility. The phosphatase and 5'-nucleotidase are shown to be activated by Mg2+ and Ca2+.
D015720:5'-Nucleotidase; D000469:Alkaline Phosphatase / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002415:Cats; D004789:Enzyme Activation; D005260:Female; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008465:Mechanoreceptors / Q000201:enzymology*; D009708:Nucleotidases / Q000378:metabolism*; D013379:Substrate Specificity
D009708:Nucleotidases; D000469:Alkaline Phosphatase; D015720:5'-Nucleotidase; D008274:Magnesium; D002118:Calcium
Shchelochnye fosfomonogidrolazy telets Pachini.