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

Authordc.contributor.authorSandoval, S. 
Authordc.contributor.authorGarcía Nannig, Lorena es_CL
Authordc.contributor.authorMancilla, Marta es_CL
Authordc.contributor.authorKettlun, Ana María es_CL
Authordc.contributor.authorCollados, L. E. es_CL
Authordc.contributor.authorChayet, L. es_CL
Authordc.contributor.authorAlvarez, A. es_CL
Authordc.contributor.authorTraverso Cori, A. es_CL
Authordc.contributor.authorValenzuela Pedevila, María Antonieta es_CL
Cita de ítemdc.identifier.citationINTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY 28 (5): 591-599es_CL
General notedc.descriptionArtículo de publicación ISIes_CL
Abstractdc.description.abstractEcto-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 substrates and bivalent cations, The aim of this work was to demonstrate the presence of apyrase as an ecto-enzyme in the rat kidney, ATPase-ADPase activities of the renal microvillar membrane preparation, which correspond to 'right side out' membranes, were characterized, The detection of ATP-diphosphohydrolase in the renal vasculature was done through perfusion of isolated rat kidney, ATPase-ADPase activities of the microvillar membrane preparation and apyrase share similar kinetic properties, These include: low substrate and bivalent metal specificities and insensitivity towards inhibitors like: oligomycin, ouabain, verapamil, levamisole and Ap(5)A. The M(r) of native ATPase and ADPase activities,vas determined by the Co-60 irradiation-inactivation technique being around 65 kDa for both hydrolytic activities, Immunowestern blot analysis also supports the presence of apyrase in microvilli, Perfusion of isolated rat kidney with ATP and ADP, in the presence or absence of different inhibitors or apyrase antibodies indicated the existence of this enzyme in the vascular endothelium. The identification of ATP-diphosphohydrolase as an ecto-enzyme both in microvilli and vasculature support the proposal that the enzyme may have an important role in the extracellular metabolism of nucleotides.es_CL
Títulodc.titleATP-diphosphohydrolase activity in rat renal microvillar membranes and vascular tissuees_CL
Document typedc.typeArtículo de revistaes_CL

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