Inorganic pyrophosphatase in isolated enamel organ and odontoblasts from the rat incisor.
The inorganic pyrophosphatase (PPiase) activity was determined by a colorimetric method in the odontoblasts and the parts of the enamel organ related to enamel matrix formation and enamel maturation. The effects on PPi hydrolysis by EDTA, R 8231, urea and heat treatment were found to be almost identical to those reported for nonspecific alkaline phosphatase (APase) in the same tissues. The Mg2+ activation curve for PPiase was also similar. Like those of APase, these characteristics of PPiase activity were identical in the three locations studied. It is suggested that the close similarity in the properties of PPiase and APase is due to activity of the same enzyme, a concept which is in agreement with recent biochemical and histochemical studies of calcification.
D000818:Animals; D004492:Edetic Acid / Q000494:pharmacology; D004658:Enamel Organ / Q000201:enzymology*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007180:Incisor / Q000201:enzymology*; D008274:Magnesium / Q000494:pharmacology; D008297:Male; D009804:Odontoblasts / Q000201:enzymology*; D011755:Pyrophosphatases / Q000378:metabolism*; D051381:Rats; D013773:Tetramisole / Q000031:analogs & derivatives* / Q000494:pharmacology; D014083:Tooth Germ / Q000201:enzymology*; D014508:Urea / Q000494:pharmacology
D014508:Urea; D004492:Edetic Acid; D013773:Tetramisole; D011755:Pyrophosphatases; D008274:Magnesium