Abstract
Quantitative electrophoretic studies of the three allozymes of glucose phosphate isomerase (GPI-1) produced byGpi-1s a/Gpi-1sc heterozygous mice revealed two opposing influences on GPI-1 activity. First, the GPI-1 AC heterodimer is less stable than GPI-1 AA but more stable than the GPI-1 CC homodimer. Second, a genetic determinant that maps close to or within theGpi-1s structural gene causes elevated activity of GPI-1 AC and probably also GPI-1 CC 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.
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This study was begun while JDW was at the MRC Radiobiology Unit and continued at the Department of Obstetrics and Gynaecology of the University of Edinburgh, where it was supported, in part, by a grant from the Moray Endowment Fund.
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West, J.D., Leask, R., Flockhart, J.H. et al. High activity of an unstable form of glucose phosphate isomerase in the mouse. Biochem Genet 25, 543–561 (1987). https://doi.org/10.1007/BF00554356
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DOI: https://doi.org/10.1007/BF00554356