In:
Development, The Company of Biologists, Vol. 97, No. 1 ( 1986-09-01), p. 225-237
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 (1) oocyte coded, (2) encoded by the embryonic, maternally derived Gpi-1sa allele and (3) encoded by the embryonic, paternally derived Gpi-1sb allele. The oocyte-coded GPI-1 activity is stable until days and then declines and is exhausted by to 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 -day embryos. Total GPI-1 activity falls to a minimum around to 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 days p.c. The method of analysis described is applicable to other dimeric enzymes with electrophoretic variants.
Type of Medium:
Online Resource
ISSN:
0950-1991
,
1477-9129
DOI:
10.1242/dev.97.1.225
Language:
English
Publisher:
The Company of Biologists
Publication Date:
1986
detail.hit.zdb_id:
2007916-3
SSG:
12
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