High activity of an unstable form of glucose phosphate isomerase in the mouse.
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.
West
J D
JD
Department of Obstetrics and Gynaecology, University of Edinburgh, Scotland.
Leask
R
R
Flockhart
J H
JH
Fisher
G
G
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
D005956:Glucose-6-Phosphate Isomerase