Now showing items 1-6 of 6

    • ATP-diphosphohydrolase activity in rat renal microvillar membranes and vascular tissue 

      Sandoval, S.; García Nannig, Lorena; Mancilla, Marta; Kettlun, Ana María; Collados, L. E.; Chayet, L.; Alvarez, A.; Traverso Cori, A.; Valenzuela Pedevila, María Antonieta (PERGAMON-ELSEVIER SCIENCE LTD, 1996-05)
      Ecto-nucleotidases may have a role in the regulation of purinoceptor-mediated responses. ATP-diphosphohydrolase or apyrase has been described as an ecto-nucleotidase, which is characterized by a low specificity for its ...
    • ATP-diphosphophydrolase activin in rat heart tissue 

      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 ...
    • Changes in apyrase activity in uterus and mammary gland during the lactogenic cycle 

      Valenzuela, M. A.; Collados, L.; Kettlun, A. M.; Mancilla, M.; Puente, J.; Aranda, E.; Chayet, L.; Alvarez, A.; Traverso Cori, A. (1992)
      1. 1. The purpose of this present research was to explore the possible roles of ATP-diphosphohydrolase (apyrase) in two tissues with high energetic demands during cell proliferation and differentiation. 2. 2. Changes in ...
    • Characterization of ATP-diphosphohydrolase from rat mammary gland 

      Alvarez, A.; Chayet, L.; Galleguillos, M.; García Nannig, Lorena; Kettlun, Ana María; Collados, L. E.; Traverso Cori, A.; Mancilla, M.; Valenzuela Pedevila, María Antonieta (PERGAMON-ELSEVIER SCIENCE LTD, 1996-01)
      ATP-diphosphohydrolase (or apyrase) hydrolyses nucleoside di- and triphosphates in the presence of millimolar concentration of divalent cations. It is insensitive towards sulfhydryl and aliphatic hydroxyl-selective reagents ...
    • Comparison of the biochemical properties, regulation and function of ATP-diphosphohydrolase from human placenta and rat kidney 

      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 ...
    • HUMAN PLACENTAL ATP-DIPHOSPHOHYDROLASE - BIOCHEMICAL .CHARACTERIZATION, REGULATION AND FUNCTION 

      Kettlun, Ana María; Alvarez, A.; Quintar, R.; Valenzuela Pedevila, María Antonieta; Collados, L. E.; Aranda, E.; Banda, A.; Chayet, L.; Chiong Lay, Mario; Mancilla, Marta; Traverso Cori, A. (PERGAMON-ELSEVIER SCIENCE LTD, 1994-03)
      1. Kinetic and physico-chemical studies on human placental microsomal fraction confirmed that the ATPase and ADPase activities detected in this fraction correspond to the enzyme ATP-diphosphohydrolase or apyrase (EC 3.6.1.5). ...