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

doi:10.1016/0024-3205(90)90505-L

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

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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 language	English (US)
Pages (from-to)	1903-1912
Number of pages	10
Journal	Life Sciences
Volume	46
Issue number	26
DOIs	https://doi.org/10.1016/0024-3205(90)90505-L
State	Published - 1990
Externally published	Yes

ASJC Scopus subject areas

Pharmacology

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10.1016/0024-3205(90)90505-L

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

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.",

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T1 - Influence of acute metabolic acidosis on the monomer and polymer forms of renal phosphate-dependent glutaminase

AU - Hortelano, Paloma

AU - García-Salguero, Leticia

AU - Lupiáñez, JoséA

AU - Alleyne, George A O

PY - 1990

Y1 - 1990

N2 - 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.

AB - 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.

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

Abstract

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