Expression of paternal glucose phosphate isomerase-1 (Gpi-1) in preimplantation stages of mouse embryos

1971 ◽  
Vol 26 (1) ◽  
pp. 153-158 ◽  
Author(s):  
V.M. Chapman ◽  
W.K. Whitten ◽  
F.H. Ruddle
Keyword(s):  
Mouse Embryos ◽  
Glucose Phosphate Isomerase ◽  
Glucose Phosphate

scholarly journals The transition from oocyte-coded to embryo-coded glucose phosphate isomerase in the early mouse embryo

Development ◽  
1983 ◽  
Vol 78 (1) ◽  
pp. 127-140
Author(s):  
John D. West ◽  
J. F. Green
Keyword(s):  
Cellulose Acetate ◽  
Mouse Embryo ◽  
Mouse Embryos ◽  
Glucose Phosphate Isomerase ◽  
Cellulose Acetate Electrophoresis ◽  
Early Mouse Embryo ◽  
Glucose Phosphate ◽  
Early Mouse

The proportions of glucose phosphate isomerase (GPI-1) allozymes produced by early (Gpi-1sa/Gpi-1sb ♀ × Gpi-1sc/Gpi-1sc ♂)F1 mouse embryos were analysed by quantitative cellulose acetate electrophoresis. Technical controls showed that this system is extremely sensitive, quantitatively reproducible and quite accurate. Genetic controls established that the Gpi-1sa/Gpi-1sb mothers were homozygous for the Gpi-1tb temporal allele, that produces relatively high GPI-1 activity in the oocyte. The oocyte-coded enzyme lasted until about 5½ days post coitum (p.c.) or shortly thereafter. The maternally derived, embryonic Gpi-1s allele was expressed no earlier than the paternally derived allele. This was first expressed between 2½ and 3½ days p.c. In this cross, most of the transition from oocyte-coded to embryo-coded GPI-1 occurred between 2½ and 3½ days p.c.

Genetic differences in glucose phosphate isomerase activity among mouse embryos

Development ◽  
1989 ◽  
Vol 107 (3) ◽  
pp. 465-472
Author(s):  
J.D. West ◽  
J.H. Flockhart
Keyword(s):  
Early Embryo ◽  
Mouse Embryos ◽  
Activity Level ◽  
Stable Form ◽  
Glucose Phosphate Isomerase ◽  
High Group ◽  
Isomerase Activity ◽  
Glucose Phosphate ◽  
Early Embryos ◽  
Low Levels

We have compared mouse embryos of three heterozygous, congenic genotypes (with high, medium and low levels of oocyte-coded glucose phosphate isomerase (GPI-1) activity respectively) to test whether 1) the survival time of oocyte-coded GPI-1 activity in the early embryo is affected by its activity level in the oocyte and 2) whether embryo-coded GPI-1 is detected earlier in embryos that inherit low levels of oocyte-coded GPI-1. The oocyte-coded GPI-1 was entirely GPI-1A allozyme in the high and medium groups but was the less stable GPI-1C allozyme in the low group. We determined total GPI-1 activity and the ratio of different GPI-1 allozymes in early embryos and calculated the activity of oocyte-coded and embryo-coded GPI-1. In all three groups, the oocyte-coded enzyme activity remained at a more or less constant level for the first 21 1/2 days. Some oocyte-coded GPI-1 remained in 4 1/2 day embryos from the high and medium groups but was gone by 5 1/2 days. Very little remained in 4 1/2 day embryos that inherited low levels of a less stable form of the enzyme (GPI-1C allozyme). Despite a 4- to 5-fold difference in initial oocyte-coded GPI-1 activity, no differences were seen among the three genotypically distinct groups of embryos in the time of activation of the embryonic Gpi-1s genes. The embryo-coded GPI-1 was first detectable in 3 1/2 day compacted morulae in all three groups. The level of oocyte-coded GPI-1, in the high group, when embryo-coded GPI-1 was first detected was higher than the level in the low group at any stage prior to detection of embryo-coded GPI-1.(ABSTRACT TRUNCATED AT 250 WORDS)

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

Development ◽  
1986 ◽  
Vol 97 (1) ◽  
pp. 225-237
Author(s):  
John D. West ◽  
Rosemary Leask ◽  
J. F. Green
Keyword(s):  
Gene Expression ◽  
Electrophoretic Analysis ◽  
Mouse Embryos ◽  
Gene Products ◽  
Glucose Phosphate Isomerase ◽  
Electrophoretic Variants ◽  
Glucose Phosphate

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 2½ days and then declines and is exhausted by 5½ to 6½ 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 2½-day embryos. Total GPI-1 activity falls to a minimum around 3½ to 4½ 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) hat there is a mechanism for the removal of oocyte-coded gene products at around 2½ days p.c. The method of analysis described is applicable to other dimeric enzymes with electrophoretic variants.

Characterization of the 5′ end of the gene for human glucose phosphate isomerase (GPI)

Genomics ◽  
1990 ◽  
Vol 7 (4) ◽  
pp. 638-643 ◽  
Author(s):  
James I.H. Walker ◽  
Pelin Faik ◽  
Michael J. Morgan
Keyword(s):  
Glucose Phosphate Isomerase ◽  
Glucose Phosphate

Comparison of human and murine isolates of Schistosoma mansoni from Richard-Toll, Senegal, by isoelectric focusing

1997 ◽  
Vol 71 (2) ◽  
pp. 175-181 ◽  
Author(s):  
M. Sène ◽  
P. Brémond ◽  
J.P. Hervé ◽  
V.R. Southgate ◽  
B. Sellin ◽  
...  
Keyword(s):  
Genetic Variation ◽  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Schistosoma Mansoni ◽  
Isoelectric Focusing ◽  
Glucose Phosphate Isomerase ◽  
Glucose Phosphate ◽  
Enzyme Systems ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Arvicanthis Niloticus

AbstractStudies on human and murine isolates of Schistosoma mansoni, from Richard-Toll, Senegal, were carried out by isoelectric focusing in polyacrylamide gels. Seven enzyme systems; lactate dehydrogenase (LDH), malate dehydrogenase (MDH), glucose-6-phosphate dehydrogenase (G6PD), acid phosphatase (AcP), hexokinase (HK), glucose phosphate isomerase (GPI), and phosphoglucomutase (PGM), were used to compare the two isolates. All systems tested, apart from LDH, were found to be polymorphic for both isolates. Interestingly, one phenotype is more frequent than the remainder. The results show that there is no significant genetic variation between the S. mansoni isolates from man and the rodents, Arvicanthis niloticus and Mastomys huberti.

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