Influence of acute metabolic acidosis on the monomer and polymer forms of renal phosphate-dependent glutaminase

Paloma Hortelano, Leticia García-Salguero, JoséA Lupiáñez, George A O Alleyne

Research output: Contribution to journalArticlepeer-review

Abstract

Phosphate-dependent glutaminase (PDG) was measured in kidney cortex homogenates and mitochondria from control and acutely acidotic rats. The effect of plasma from acutely acidotic rats on PDG activity in homogenates from normal rats was also studied. Acidosis or incubation in acidotic plasma enhanced enzyme activity when measured at 1.0 mM but not at 20.0 mM glutamine. This effect was not due to increased mitochondrial permeability since similar results were obtained after solubilization of the enzyme with Triton X-100. Increased enzyme activity was observed with either the Tris (monomer) form or the borate (polymer) form of the enzyme, indicating that enhanced activity is not due to polymerization but probably to a conformational change in the enzyme such that the Km for glutamine is lowered.

Original languageEnglish (US)
Pages (from-to)1903-1912
Number of pages10
JournalLife Sciences
Volume46
Issue number26
DOIs
StatePublished - 1990
Externally publishedYes

ASJC Scopus subject areas

  • Pharmacology

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