PMID: 37914Jul 11, 1979

Identification, characterization and localization of a (Ca2+ + Mg2+)-activated purine nucleoside triphosphate phosphohydrolase from calcifying cartilage

Biochimica Et Biophysica Acta
S E Kahn, C Arsenis


A purine nucleoside triphosphate phosphohydrolase (unspecified diphosphate phosphohydrolase, EC was chromatographically separated from the bulk of alkaline phosphatase activity by gel filtration chromatography of butanol and EDTA extracts of fracture callus and bovine epiphyseal cartilage. The callus enzyme differed from alkaline phosphatase in a variety of characteristics. The purine nucleoside triphosphate phosphatase hydrolyzed a more specific group of substrates, required Ca2+ and Mg2+ for optimal activity, remained unaffected by a potent alkaline phosphatase inhibitor, and demonstrated a narrower range of optimal pH for catalytic activity. The enzyme was localized in the microsomal pellet following subcellular fractionation of callus chondrocytes. These characteristics indicate a role for the enzyme in Ca2+ transport.


Sep 1, 1976·The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society·G Granström, A Linde
May 1, 1978·The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society·G GranströmH Nygren
Oct 13, 1977·Differentiation; Research in Biological Diversity·C Arsenis, S M Huang
Nov 1, 1970·Proceedings of the National Academy of Sciences of the United States of America·S Y AliH C Anderson


Jan 1, 1986·Ultrastructural Pathology·A StarkJ L Ericsson

Related Concepts

Ca(2+)-Transporting ATPase
Alkaline Phosphatase
Bone Mineralization
Bone Callus
Structure of Articular Cartilage
Molecular Sieve Chromatography
Hydrogen-Ion Concentration

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