Quantification of the transition from oocyte-coded to embryo-coded glucose phosphate isomerase in mouse embryos

J D West, R Leask, J F Green

Research output: Contribution to journalArticlepeer-review

Abstract

A quantitative electrophoretic analysis of glucose phosphate isomerase (GPI-1) allozymes produced by heterozygous Gpi-1sa/Gpi-1sb mouse embryos has enabled us to estimate separately the contributions of GPI-1 enzyme that were oocyte coded, encoded by the embryonic, maternally derived Gpi-1sa allele and encoded by the embryonic, paternally derived Gpi-1sb allele. The oocyte-coded GPI-1 activity is stable until 2 1/2 days and then declines and is exhausted by 5 1/2 to 6 1/2 days post coitum (p.c.). The maternally and paternally derived Gpi-1s alleles are probably usually activated synchronously but several possible exceptions were observed. This activation was first detected in 2 1/2-day embryos. Total GPI-1 activity falls to a minimum around 3 1/2 to 4 1/2 days, even though embryonic gene expression has already begun. The profile of oocyte-coded GPI-1 activity is consistent with the suggestion (Harper & Monk, 1983) that there is a mechanism for the removal of oocyte-coded gene products at around 2 1/2 days p.c. The method of analysis described is applicable to other dimeric enzymes with electrophoretic variants.

Original languageEnglish
Pages (from-to)225-37
Number of pages13
JournalJournal of embryology and experimental morphology
Volume97
Publication statusPublished - Sep 1986

Keywords

  • Animals
  • Embryo, Mammalian
  • Genes
  • Glucose-6-Phosphate Isomerase
  • Isoenzymes
  • Mice
  • Oocytes

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