Now showing items 1-4 of 4

    • Espinosa, Victoria; Galleguillos, M.; Mancilla, Marta; Garrido, J.; Kettlun, Ana María; Collados, L. E.; Chayet, L.; García Nannig, Lorena; Traverso Cori, A.; Valenzuela Pedevila, María Antonieta (ACADEMIC PRESS AUST, 1996-08)
      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 ...
    • Valenzuela Pedevila, María Antonieta; Kettlun, Ana María; Sandoval, S.; García Nannig, Lorena; Mancilla, Marta; Neckelmann, G.; Chayet, L.; Alvarez, A.; Cuevas, F.; Collados, L. E.; Espinosa, Victoria; Traverso Cori, A.; Bravo, I.; Acevedo, C. G.; Aranda, E. (ASSOC BRAS DIVULG CIENTIFICA, 1996-05)
      ATP-diphosphohydrolase (apyrase, EC 3.6.1.5) has both ATPase and ADPase activity that are stimulated by bivalent metals, with Ca2+ being the most effective. The possible physiological function of this enzyme, associated ...
    • Espinosa, Victoria; Kettlun, Ana María; Zanocco Loyola, Antonio; Cardemil, E.; Valenzuela, A. M. (PERGAMON-ELSEVIER SCIENCE LTD, 2003-05)
      Comparative studies of intrinsic and extrinsic fluorescence of apyrases purified from two potato tuber varieties (Pimpernel and Desiree) were performed to determine differences in the microenvironment of the nucleotide ...
    • Espinosa, Victoria; Kettlun, Ana María; Zanocco Loyola, Antonio; Cardemil, E.; Valenzuela Pedevila, María Antonieta (PERGAMON-ELSEVIER SCIENCE LTD, 2000-08)
      Chemical modification of potato apyrase suggests that tryptophan residues are close to the nucleotide binding site. K-d values (+/- Ca2+) for the complexes of apyrase with the non-hydrolysable phosphonate adenine nucleotide ...