The activation of chick alkaline phosphatase by calmodulin.
Calmodulin, an activator protein in most calcium-dependent processes, was isolated to apparent homogeneity from the femurs of 1-day old chicks using phenyl-Sepharose and high performance liquid chromatography. The purified calmodulin was found to produce a 6-fold increase in the activity of alkaline phosphatase isolated from the same source. A Ca2+ concentration of 10(-5) M was required for the activation. Purification of alkaline phosphatase involved acetone precipitation, DEAE-Sephacel and Sephadex G-200 column chromatography. The enzyme was purified to 540-fold and had a specific activity of 10.75 U/mg protein.
Sivanaesan
L
L
Department of Biochemistry, Faculty of Medicine, University of Malaya, Kuala Lumpur.
Kwan
T K
TK
Perumal
R
R
D000469:Alkaline Phosphatase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D001842:Bone and Bones / Q000737:chemistry; D002147:Calmodulin / Q000302:isolation & purification / Q000502:physiology*; D002645:Chickens; D002853:Chromatography, Liquid; D004789:Enzyme Activation / Q000502:physiology; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism
D002147:Calmodulin; D000469:Alkaline Phosphatase; D010727:Phosphoric Diester Hydrolases