Now showing items 1-9 of 9

    • 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 ...
    • 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 ...
    • Pieber, M.; Valenzuela Pedevila, María Antonieta; Kettlun, Ana María; Mancilla, Marta; Aranda, E.; Collados, L. E.; Traverso Cori, A. (PERGAMON-ELSEVIER SCIENCE LTD, 1991)
      1. Calcium-stimulated ATPase-ADPase activities were studied in a microsomal fraction of rat placental tissue. 2. The kinetic characteristics correspond to those of ATP-diphosphohydrolase, also known as apyrase (E.C. ...
    • 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 ...
    • 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 ...
    • Cartier Rovirosa, Luis; García Nannig, Lorena; Kettlun, Ana María; Castañeda, P.; Collados, L. E.; Vásquez, F.; Giraudon, P.; Belin, M. F.; Valenzuela Pedevila, María Antonieta (TAYLOR & FRANCIS AS, 2004-04)
      The cerebrospinal fluid (CSF) is in direct contact with the extracellular space of the CNS, thus biochemical processes in the CNS could potentially be reflected in the CSF. Changes in extracellular matrix (ECM) proteins ...
    • Valenzuela Pedevila, María Antonieta; Cartier Rovirosa, Luis; Collados, L. E.; Kettlun, Ana María; Araya, F.; Concha, C.; Flores, L.; Wolf, M. E.; Mosnaim, A. D. (P J D PUBLICATIONS LTD, 1999)
      We have studied the enzymatic gelatinolytic activity of matrix metalloproteinases (MMPs) present in cerebrospinal fluid (CSF) of samples obtained from 67 individuals, twenty-one nonneurological patients (considered controls) ...
    • 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). ...
    • Kettlun, Ana María; Cartier Rovirosa, Luis; García Nannig, Lorena; Collados, L. E.; Vásquez, F.; Ramírez, E.; Valenzuela Pedevila, María Antonieta (PERGAMON-ELSEVIER SCIENCE LTD, 2003-05-09)
      The tropical spastic paraparesis or human T-cell lymphotropic virus associated myelopathy (TSP/HAM), has been related with an overexpression of matrix metalloproteinases (MMPs), especially MMP-9. Initial studies of reverse ...