Glucose phosphate isomerase enzyme-activity mutants inMus musculus: Genetical and biochemical characterization

1990 ◽  
Vol 28 (1-2) ◽  
pp. 97-110 ◽  
Author(s):  
Walter Pretsch ◽  
Siegbert Merkle
Keyword(s):  
Enzyme Activity ◽  
Biochemical Characterization ◽  
Glucose Phosphate Isomerase ◽  
Glucose Phosphate

scholarly journals Induction of glycolytic enzyme synthesis in proliferating fibroblasts. Study of phosphofructokinase, glucose phosphate isomerase and pyruvate kinase

1983 ◽  
Vol 214 (1) ◽  
pp. 195-201 ◽  
Author(s):  
M C Meienhofer ◽  
J C Dreyfus ◽  
A Kahn
Keyword(s):  
Enzyme Activity ◽  
Pyruvate Kinase ◽  
Specific Activity ◽  
Human Fibroblasts ◽  
Glycolytic Enzymes ◽  
Resting Cells ◽  
Glucose Phosphate Isomerase ◽  
Antigen Concentration ◽  
Quiescent Cells ◽  
Glucose Phosphate

Specific activity of phosphofructokinase is 7-8-fold higher in exponentially growing human fibroblasts than in quiescent cells, but the difference is considerably less pronounced for two other glycolytic enzymes, glucose phosphate isomerase and pyruvate kinase. The ratio of the F-type to L-type phosphofructokinase subunits is essentially the same in growing and resting cells, 4:1. F-type-phosphofructokinase-related antigen concentration is decreased in resting cells as compared with proliferating fibroblasts, but relatively less than the enzyme activity; the ratio of the enzyme activity to the antigen concentration (immunological specific activity) is therefore lower in resting than in growing fibroblasts. Synthesis of phosphofructokinase, as a percentage of the total protein synthesis, is about 30-fold greater during the proliferative phase than in quiescent cells, but this difference is only 3-4-fold for glucose phosphate isomerase and pyruvate kinase. Modulation of the synthesis of phosphofructokinase therefore seems to be responsible for the changes of its specific activity in function of cell proliferation. The appearance of some inactive cross-reacting material in quiescent cells is probably due to post-translational alteration of the pre-synthesized molecules. Compared with other glycolytic enzymes, such as glucose phosphate isomerase and pyruvate kinase, phosphofructokinase seems to be the (or one of the) preferential target of glycolytic induction in proliferating cells.

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.

scholarly journals Extracellular α-Galactosidase from Trichoderma sp. (WF-3): Optimization of Enzyme Production and Biochemical Characterization

2015 ◽  
Vol 2015 ◽  
pp. 1-6 ◽  
Author(s):  
Aishwarya Singh Chauhan ◽  
Arunesh Kumar ◽  
Nikhat J. Siddiqi ◽  
B. Sharma
Keyword(s):  
Enzyme Activity ◽  
Enzyme Assay ◽  
Biochemical Characterization ◽  
Catalytic Efficiency ◽  
Culture Conditions ◽  
Significant Loss ◽  
Trichoderma Sp ◽  
Rate Of Reaction ◽  
Higher Temperature ◽  
Substrate Concentrations

Trichoderma spp. have been reported earlier for their excellent capacity of secreting extracellular α-galactosidase. This communication focuses on the optimization of culture conditions for optimal production of enzyme and its characterization. The evaluation of the effects of different enzyme assay parameters such as stability, pH, temperature, substrate concentrations, and incubation time on enzyme activity has been made. The most suitable buffer for enzyme assay was found to be citrate phosphate buffer (50 mM, pH 6.0) for optimal enzyme activity. This enzyme was fairly stable at higher temperature as it exhibited 72% activity at 60°C. The enzyme when incubated at room temperature up to two hours did not show any significant loss in activity. It followed Michaelis-Menten curve and showed direct relationship with varying substrate concentrations. Higher substrate concentration was not inhibitory to enzyme activity. The apparent Michaelis-Menten constant (Km), maximum rate of reaction (Vmax), Kcat, and catalytic efficiency values for this enzyme were calculated from the Lineweaver-Burk double reciprocal plot and were found to be 0.5 mM, 10 mM/s, 1.30 U mg−1, and 2.33 U mg−1 mM−1, respectively. This information would be helpful in understanding the biophysical and biochemical characteristics of extracellular α-galactosidase from other microbial sources.

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

Analyzing Glucose Phosphate Isomerase Isozymes in Chimeric Mouse Tissues by Electrophoresis

2008 ◽  
Vol 2008 (10) ◽  
pp. pdb.prot4813-pdb.prot4813
Author(s):  
A. Nagy ◽  
M. Gertsenstein ◽  
K. Vintersten ◽  
R. Behringer
Keyword(s):  
Chimeric Mouse ◽  
Glucose Phosphate Isomerase ◽  
Glucose Phosphate ◽  
Mouse Tissues
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