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Literature DB >> 6444839

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

Abstract

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.

Entities: Chemical Species

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Year: 1980 PMID： 6444839 DOI： 10.1007/bf02408608

Source DB: PubMed Journal: Calcif Tissue Int ISSN： 0171-967X Impact factor: 4.333

14 in total

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

1. A rapid and sensitive radiometric assay for adenosine triphosphatase activity using Cerenkov radiation.

2. Pyrophosphatase and ATPase of isolated cartilage matrix vesicles.

3. EXCRETION OF INORGANIC PYROPHOSPHATE IN HYPOPHOSPHATASIA.

4. Further studies on the incorporation of inorganic phosphate into calf-intestinal alkaline phosphatase.

5. Inhibition studies of alkaline phosphatase in hard tissue-forming cells.

6. The effect of vitamin D on enzyme activities in the mucosal cells of the chick small intestine.

7. Ca-2+, Mg-2+-activated ATPase and alkaline phosphatase of developing chick femora.

8. Relation between alkaline phosphatase and Ca 2+ -ATPase in calcium transport.

9. Properties of a Ca 2+ -and Mg 2+ -activated ATP-hydrolyzing enzyme in rat kidney cortex.

10. Organic pyrophosphates as substrates for human alkaline phosphatases.

1. Effects of cortisol and fluoride on ion-transporting ATPase activities in cultured osteoblastlike cells.

2. Ion-transporting ATPases and matrix mineralization in cultured osteoblastlike cells.