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. 1987 Aug;25(7-8):543-61.
doi: 10.1007/BF00554356.

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

J D West  1 , R Leask, J H Flockhart, G Fisher
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High activity of an unstable form of glucose phosphate isomerase in the mouse

J D West et al. Biochem Genet. 1987 Aug.

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.

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References

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