Affordable Access

Effect of inorganic phosphate on the self-associating properties of glutathione reductase from Spirulina maxima.

Authors
  • Rendón, J L
  • Mendoza-Hernández, G
Type
Published Article
Journal
Biochemistry and molecular biology international
Publication Date
Nov 01, 1993
Volume
31
Issue
4
Pages
701–708
Identifiers
PMID: 8298499
Source
Medline
License
Unknown

Abstract

In the presence of millimolar concentrations of inorganic phosphate, native Spirulina maxima glutathione reductase (NAD[P]H:GSSG oxidoreductase EC 1.6.4.2.) changes its aggregation state. The oligomeric structure of the enzyme was notably dependent upon phosphate molarity, ranging from a dimer-tetramer equilibrium at relatively low phosphate concentrations into a tetramer-octamer equilibrium at moderate or high phosphate concentrations. In spite of the changes in quaternary structure, the tetramer remains as the most stable and abundant species. Sodium chloride solutions were not able to produce a similar effect, thus discarding an unspecific ionic strength effect.

Report this publication

Statistics

Seen <100 times