High activity of an unstable form of glucose phosphate isomerase in the mouse

J D West, R Leask, J H Flockhart, G Fisher

Research output: Contribution to journalArticlepeer-review

Abstract

Quantitative electrophoretic studies of the three allozymes of glucose phosphate isomerase (GPI-1) produced by Gpi-1sa/Gpi-1sc heterozygous mice revealed two opposing influences on GPI-1 activity. First, the GPI-1AC heterodimer is less stable than GPI-1AA but more stable than the GPI-1CC homodimer. Second, a genetic determinant that maps close to or within the Gpi-1s structural gene causes elevated activity of GPI-1AC and probably also GPI-1CC dimers. The relative lability of these allozymes masks this elevated activity in some tissues but the effect is probably ubiquitous. The significance of these observations is discussed.

Original languageEnglish
Pages (from-to)543-61
Number of pages19
JournalBiochemical genetics
Volume25
Issue number7-8
Publication statusPublished - Aug 1987

Keywords

  • Alleles
  • Animals
  • Electrophoresis, Cellulose Acetate
  • Enzyme Stability
  • Female
  • Gene Expression Regulation
  • Genetic Linkage
  • Genotype
  • Glucose-6-Phosphate Isomerase
  • Male
  • Mice
  • Mice, Inbred Strains
  • Organ Specificity

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