Glucose Phosphate Isomerase Activity in C57BL/6 and A Mice of Different Ages

Gerontology ◽  
1985 ◽  
Vol 31 (5) ◽  
pp. 315-320 ◽  
Author(s):  
Carol M. Warner ◽  
Carol J. Briggs ◽  
Doris Balinsky ◽  
Terry E. Meyer
Keyword(s):  
Glucose Phosphate Isomerase ◽  
Isomerase Activity ◽  
Glucose Phosphate ◽  
Different Ages

Glucose phosphate isomerase activity in mouse and human eggs and pre-embryos

1989 ◽  
Vol 4 (1) ◽  
pp. 82-85 ◽  
Author(s):  
John D. West ◽  
Jean H. Flockhart ◽  
Roslyn R. Angell ◽  
Stephen G. Hillier ◽  
Samuel S. Thatcher ◽  
...  
Keyword(s):  
Glucose Phosphate Isomerase ◽  
Isomerase Activity ◽  
Glucose Phosphate

scholarly journals Genetic and Molecular Mechanisms of the Congenital Defects in Glucose Phosphate Isomerase Activity: Studies of Four Families

1977 ◽  
Vol 11 (11) ◽  
pp. 1123-1129 ◽  
Author(s):  
A Kahn ◽  
J P M Van Biervliet ◽  
J L Vives-Corrons ◽  
D Cottreau ◽  
G E J Staal
Keyword(s):  
Molecular Mechanisms ◽  
Congenital Defects ◽  
Glucose Phosphate Isomerase ◽  
Isomerase Activity ◽  
Glucose Phosphate

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)

scholarly journals Non-additive inheritance of glucose phosphate isomerase activity in mice heterozygous at the Gpi-1s structural locus

1989 ◽  
Vol 54 (1) ◽  
pp. 27-36 ◽  
Author(s):  
John D. West ◽  
Jean H. Flockhart
Keyword(s):  
Catalytic Activity ◽  
Heat Stability ◽  
Glucose Phosphate Isomerase ◽  
Contributing Factors ◽  
Structural Locus ◽  
Relative Stabilities ◽  
Isomerase Activity ◽  
Glucose Phosphate ◽  
Additive Inheritance

SummaryThe activity of blood glucose phosphate isomerase (GPI-1) in mice heterozygous for various alleles at the Gpi-1s structural locus (heterozygotes a/b, a/c and b/c) was significantly higher than expected, on the basis of additive inheritance, from the levels in parental homozygotes. Moreover, the GPI-1 activity was higher in a/b heterozygotes than in either parent (heterosis). Studies of heat stability with kidney homogenates revealed that the relative stabilities of GPI-1 dimers was AA > AB > BB > AC ≥ BC > CC. Differences in dimer stabilities in vivo would affect the total GPI-1 levels in heterozygotes and could account for non-additive inheritance but would be insufficient to explain heterosis for GPI-1 activity. Other possible contributing factors include unequal production or stability of monomers, or higher catalytic activity of heterodimers. Monomers could also associate non-randomly but this would not be sufficient to explain heterosis. It is clear that non-additive inheritance patterns may be produced by variants of either structural or regulatory genes.

scholarly journals GPI expression in female germ cells of the mouse

1981 ◽  
Vol 37 (3) ◽  
pp. 303-309 ◽  
Author(s):  
Anne McLaren ◽  
Mia Buehr
Keyword(s):  
Structural Gene ◽  
Germ Cells ◽  
Gene Complex ◽  
Glucose Phosphate Isomerase ◽  
Specific Expression ◽  
Isomerase Activity ◽  
Glucose Phosphate ◽  
Form Part ◽  
Genetically Determined

SUMMARYThe genetically determined oocyte-specific expression of glucose-phosphate isomerase activity in the mouse is first apparent at 6 to 7 days after birth, and occurs in XO as well as in XX oocytes. The regulator locus that controls oocyte-specific expression shows the same linkage relations as the structural gene, suggesting that both form part of a Gpi-1 gene complex.

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.

Glucose Phosphate Isomerase Deficiency as a Cause of Hydrops Fetalis

1987 ◽  
Vol 316 (5) ◽  
pp. 258-261 ◽  
Author(s):  
Yaddanapudi Ravindranath ◽  
Donald E. Paglia ◽  
Indira Warrier ◽  
William Valentine ◽  
Misae Nakatani ◽  
...  
Keyword(s):  
Hydrops Fetalis ◽  
Glucose Phosphate Isomerase ◽  
Glucose Phosphate
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