Alkaline phosphatase and ATPase activities of rat bone: separation and characterization.

Extraction with Triton X-100 has proved effective in solubilizing alkaline phosphatase from rat bone particles, whereas ATPase with optimum activity at pH 8 remains attached to the bone particles. The kinetic characteristics of the ATPase activity of the Triton extracts are different from those of the same enzyme attached to bone particles, but the kinetic characteristics of the particle-bound and solubulized alkaline phosphatases are similar. The results suggest that the Triton extracts do not have true ATPase activity and provide a means of separating the ATPase and alkaline phosphatase activities.