Solubilization and partial characterization of ouabain-insensitive na -atpase from basolateral plasma membranes of the intestinal epithelial cells. Report as inadecuate




Solubilization and partial characterization of ouabain-insensitive na -atpase from basolateral plasma membranes of the intestinal epithelial cells. - Download this document for free, or read online. Document in PDF available to download.

Investigación Clínica 2009, 50 3

Author: Freddy Romero

Source: http://www.redalyc.org/articulo.oa?id=372937677004


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Investigación Clínica ISSN: 0535-5133 riclinicas@gmail.com Universidad del Zulia Venezuela Romero, Freddy Solubilization and partial characterization of ouabain-insensitive Na -ATPase from basolateral plasma membranes of the intestinal epithelial cells. Investigación Clínica, vol.
50, núm.
3, 2009, pp.
303-314 Universidad del Zulia Maracaibo, Venezuela Available in: http:--www.redalyc.org-articulo.oa?id=372937677004 How to cite Complete issue More information about this article Journals homepage in redalyc.org Scientific Information System Network of Scientific Journals from Latin America, the Caribbean, Spain and Portugal Non-profit academic project, developed under the open access initiative Invest Clin 50(3): 303 - 314, 2009 Solubilization and partial characterization of ouabain-insensitive Na -ATPase from basolateral plasma membranes of the intestinal epithelial cells. Freddy Romero. Laboratorio de Fisiología Gastrointestinal, Centro de Biofísica y Bioquímica, Instituto Venezolano de Investigaciones Científicas, Caracas, Venezuela. Key words: Na -ATPase; polyoxyethylene 9-lauryl ether (C12E9), second sodium pump, epithelial cell, small intestine, furosemide. Abstract.
It has been proposed that intestinal sodium transport is mediated by two different active mechanisms: the ouabain-sensitive Na -K -ATPase and ouabain-insensitive Na -ATPase.
In order to determine the optimum conditions to solubilize the membrane-bound Na -ATPase of enterocyte, basolateral plasma membranes were solubilized using different amounts of octyl glucoside (O.G), Tween 20, octaethylene glycol monododecyl ether (C12E8), and polyoxyethylene 9-lauryl ether (C12E9).
Solubilized fractions were assayed for protein concentration and ATPase activity and characterized by electrophoresis analysis.
Optimal solubilization of Na -ATPase was obtained after mixing of 1 mg of basolateral plasma membrane with 1.5 mg of C12E9. Under these conditions, C12E9 solubilized over 60% membrane prote...





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