PMID: 3214421Nov 1, 1988Paper

Purification of phosphate-dependent glutaminase from isolated mitochondria of Ehrlich ascites-tumour cells

The Biochemical Journal
A R QuesadaI Núñez de Castro

Abstract

Phosphate-dependent glutaminase was purified to homogeneity from isolated mitochondria of Ehrlich ascites-tumour cells. The enzyme had an Mr of 135,000 as judged by chromatography on Sephacryl S-300. SDS/polyacrylamide-gel electrophoresis displayed two protein bands, with Mr values of 64,000 and 56,000. Two major immunoreactive peptides of Mr values of 65,000 and 57,000 were found by immunoblot analysis using anti-(rat kidney glutaminase) antibodies. The concentration-dependences for both glutamine and phosphate were sigmoidal, with S0.5 values of 7.6 mM and 48 mM, and Hill coefficients of 1.5 and 1.6, respectively. The glutaminase pH optimum was 9. The activation energy of the enzymic reaction was 58 kJ/mol. The enzyme showed a high specificity towards glutamine. A possible explanation for the different kinetic behaviour found for purified enzyme and for isolated mitochondria [Kovacević (1974) Cancer Res. 34, 3403-3407] should be that a conformational change occurs when the enzyme is extracted from the mitochondrial inner membrane.

Citations

May 12, 2009·Neurochemistry International·Vanessa de la RosaJavier Márquez
Aug 26, 2009·The International Journal of Biochemistry & Cell Biology·José M MatésJavier Márquez
May 12, 2009·Neurochemistry International·Monika Szeliga, Marta Obara-Michlewska
Aug 1, 1992·Biochemical Medicine and Metabolic Biology·M A MedinaI Núñez de Castro
Dec 23, 1999·Pathology Oncology Research : POR·P MaityP Bhattacharya
Mar 14, 1994·FEBS Letters·J C AledoJ Márquez
Oct 18, 2000·Pathology Oncology Research : POR·P Bhattacharya, P Maity
Sep 5, 2001·The Journal of Nutrition·M A Medina
Jun 5, 1999·Molecular Genetics and Metabolism·M I Amores-Sánchez, M A Medina
Jan 1, 1990·The International Journal of Biochemistry·M A Medina, I Núñez de Castro

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