Pyrophosphatase and ATPase of isolated cartilage matrix vesicles.
Some of the characteristics of the pyrophosphatase and ATPase activities studied in isolated cartilage matrix vesicles were found to be similar to those already reported for the solubilized and purified bone alkaline phosphatase. Thus, the pH optimum of the pyrophosphatase activity responded similarly to changes in the concentration of Mg2+, Ca2+, and PPi. Further, the ATPase activity was not activated by Ca2+ in the presence of an optimal Mg2+ concentration. It is proposed that a function of the alkaline phosphatase of matrix vesicles in vivo is to hydrolyze the substrates PPi, ADP, and ATP, which are known inhibitors of calcium phosphate precipitation.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors; D000818:Animals; D002113:Calcification, Physiologic; D002118:Calcium / Q000494:pharmacology; D002356:Cartilage / Q000201:enzymology*; D002645:Chickens; D004164:Diphosphonates / Q000494:pharmacology; D004789:Enzyme Activation; D004838:Epiphyses / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D010710:Phosphates / Q000494:pharmacology; D011755:Pyrophosphatases / Q000037:antagonists & inhibitors
D004164:Diphosphonates; D010710:Phosphates; D000251:Adenosine Triphosphatases; D011755:Pyrophosphatases; D008274:Magnesium; D002118:Calcium