Browsing by Author "Mancilla, Marta"

Now showing items 1-8 of 8

    • 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 ...
    • ATPASE-ADPASE ACTIVITIES OF RAT PLACENTAL TISSUE 
      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. ...
    • Comparison of the biochemical properties, regulation and function of ATP-diphosphohydrolase from human ... 
      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). ...
    • IDENTIFICATION AND SUBCELLULAR-LOCALIZATION OF 2 ISOENZYMES OF APYRASE FROM SOLANUM-TUBEROSUM 
      Kettlun, Ana María; Leyton, Mario; Valenzuela Pedevila, María Antonieta; Mancilla, Marta; Traverso Cori, A. (PERGAMON-ELSEVIER SCIENCE LTD, 1992-06)
      Two forms of ATP-diphosphohydrolase were identified in Solanum tuberosum tuber var. Ultimus. Their hydrolytic activity ratios (ATPase/ADPase) were over 10 for form A and 1 for form B. In the potato tuber homogenate the ...
    • Partial purification and immunohistochemical localization of ATP diphosphohydrolase from Schistosoma mansoni ... 
      Vasconcelos, E. G.; Ferreira, Sergio T.; Técia, M. U.; De Souza, Wanderley; Kettlun, Ana María; Mancilla, Marta; Valenzuela Pedevila, María Antonieta; Verjovski Almeida, S. (AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 1996-09-06)
      ATP diphosphohydrolase from tegumental membranes of Schistosoma mansoni was solubilized with Triton X-100 plus deoxycholate and separated by preparative nondenaturing polyacrylamide gel electrophoresis. Two isoforms with ...
    • PURIFICATION AND CHARACTERIZATION OF 2 ISOAPYRASES FROM SOLANUM-TUBEROSUM VAR ULTIMUS 
      Kettlun, Ana María; Urra, Raúl; Leyton, Mario; Valenzuela Pedevila, María Antonieta; Mancilla, Marta; Traverso Cori, A. (PERGAMON-ELSEVIER SCIENCE LTD, 1992-11)
      Two isoenzymes of ATP-diphosphohydrolase (apyrase) were extracted and purified from S. tuberosum var. Ultimus. Their hydrolytic activity ratios (ATPase/ADPase) were 1.0 (apyrase B) and ca 15.0 (apyrase A). They were ...