Activation and specificity of alkaline phosphatase of a mineralizing collagen-rich system.
Alkaline phosphatase from tibia tendon of Meleagris gallopavo L. was highly purified. The enzyme activation by different ions was measured. Mg2+ showed a high activation with a broader spectrum of phosphomonoester hydrolization. The in vivo Mg2+ concentration was an optimum for in vitro activation.
D000469:Alkaline Phosphatase / Q000378:metabolism*; D000818:Animals; D004789:Enzyme Activation; D008274:Magnesium / Q000494:pharmacology; D013710:Tendons / Q000201:enzymology*; D014422:Turkeys
D000469:Alkaline Phosphatase; D008274:Magnesium