ATP-diphosphophydrolase activin in rat heart tissueReport as inadecuate

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Extracellular nucleotides interact with specific receptors on the cell surface and are locally metabolized by ecto-nucleotidases. Biochemical characterization of the ATPase and ADPase activities detected in rat heart sarcolemma, under conditions where mitochondrial ATPase and adenylate kinase were blocked, suppor:s our proposal that both activities correspond to a single enzyme, known as ATP-diphosphohydrolase or apyrase. The physiological function of this enzyme could be dephosphorylation of the nucleotides present in the interstitial heart compartment acting together with 5-nucleotidase. Both hydrolytic activities have similarities in: sarcolemma localization, bivalent metal ion dependence, optimum pH, effect of several amino acid residue modifiers, competitive inhibition of nucleotide analogs, and broad nucleoside di- and triphosphate specificity. The ATPase activity could not be separated from the ADPase either through isoelectrofocusing or electrophoresis under acid conditions.Nota general

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Author: Espinosa, Victoria; - Galleguillos, M.; - Mancilla, Marta; - Garrido, J.; - Kettlun, Ana María; - Collados, L. E.; - Chayet, L.;



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