Alkaline phosphatase and ATPase activities of rat bone: Separation and characterization |
| |
Authors: | A. W. Skillen M. Rahbani-Nobar |
| |
Affiliation: | (1) University Department of Clinical Biochemistry, Royal Victoria Infirmary, NE1 4LP Newcastle upon Tyne, England |
| |
Abstract: | Summary 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 solubilized 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. |
| |
Keywords: | Alkaline phosphatase ATPase Bone Triton |
本文献已被 SpringerLink 等数据库收录! |