title: High activity of an unstable form of glucose phosphate isomerase in the mouse.
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.
authors.affiliation: Department of Obstetrics and Gynaecology, University of Edinburgh, Scotland.
authors.forename: J D
authors.initials: JD
authors.lastname: West
authors.forename: R
authors.initials: R
authors.lastname: Leask
authors.forename: J H
authors.initials: JH
authors.lastname: Flockhart
authors.forename: G
authors.initials: G
authors.lastname: Fisher
mesh_terms: D000483:Alleles; D000818:Animals; D004588:Electrophoresis, Cellulose Acetate; D004795:Enzyme Stability; D005260:Female; D005786:Gene Expression Regulation; D008040:Genetic Linkage; D005838:Genotype; D005956:Glucose-6-Phosphate Isomerase / Q000235:genetics* / Q000378:metabolism; D008297:Male; D051379:Mice; D008815:Mice, Inbred Strains; D009928:Organ Specificity
chemical_list: D005956:Glucose-6-Phosphate Isomerase