Results 141 to 150 of about 39,501 (165)
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Photochemical cross-linking of guanosine 5'-triphosphate to phosphoenolpyruvate carboxykinase (GTP)
Bioconjugate Chemistry, 1992Mammalian phosphoenolpyruvate carboxykinase (PEPCK) specifically requires a guanosine or inosine nucleotide as a substrate; however, the structural basis for this nucleotide specificity is not yet known. Because affinity labels derived from guanosine have not yielded a stable, modified peptide in quantities sufficient for sequence analysis, we have ...
C T, Lewis, J M, Seyer, G M, Carlson
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Insulin and glucagon regulate cytosolic phosphoenolpyruvate carboxykinase (GTP) mRNA in rat liver
Diabetes, 1984Insulin causes a 7–10-fold decrease of both the mRNA that codes for rat hepatic phosphoenolpyruvate carboxykinase (mRNAPEPCK) and of PEPCK synthesis, provided the animals are made diabetic and fed chow. mRNAPEPCK, measured either by in vitro translation or cDNA hybridization, decreases with a half-time of 30–60 min after insulin treatment.
E, Beale +4 more
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Enzyme, 2017
The cytosolic form of phosphoenolpyruvate carboxykinase (GTP; EC 4.1.1.32) from rat liver was purified by a procedure involving affinity chromatography on agarosehydrazide- GTP. Phosphoenolpyruvate carboxykinase is retained quantitatively by the affinity medium in the presence of manganese and can be specifically eluted by a pulse of GTP.
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The cytosolic form of phosphoenolpyruvate carboxykinase (GTP; EC 4.1.1.32) from rat liver was purified by a procedure involving affinity chromatography on agarosehydrazide- GTP. Phosphoenolpyruvate carboxykinase is retained quantitatively by the affinity medium in the presence of manganese and can be specifically eluted by a pulse of GTP.
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Archives of Biochemistry and Biophysics, 1975
Abstract In vitro , 3-mercaptopicolinic acid inhibited phosphoenolpyruvate carboxykinase activity in supernatant fractions of liver, kidney cortex, and adipose tissue obtained from fasted rats. 3-Mercaptopicolinic acid also inhibited enzymatic activity in the mitochondrial and supernatant fractions of liver obtained from fasted guinea pigs.
V, Kostos +4 more
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Abstract In vitro , 3-mercaptopicolinic acid inhibited phosphoenolpyruvate carboxykinase activity in supernatant fractions of liver, kidney cortex, and adipose tissue obtained from fasted rats. 3-Mercaptopicolinic acid also inhibited enzymatic activity in the mitochondrial and supernatant fractions of liver obtained from fasted guinea pigs.
V, Kostos +4 more
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Advances in Enzyme Regulation, 1981
As can be seen from the data presented in this chapter, glucagon, epinephrine and Bt2cAMP can act directly on isolated rat hepatocytes to markedly increase the concentration of P-enolpyruvate carboxykinase mRNA. The effects of these hormones on enzyme mRNa are rapid, causing a 2–3-fold increase in 90 min of incubation.
M A, Cimbala +2 more
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As can be seen from the data presented in this chapter, glucagon, epinephrine and Bt2cAMP can act directly on isolated rat hepatocytes to markedly increase the concentration of P-enolpyruvate carboxykinase mRNA. The effects of these hormones on enzyme mRNa are rapid, causing a 2–3-fold increase in 90 min of incubation.
M A, Cimbala +2 more
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Developmental & Comparative Immunology, 2017
Phosphoenolpyruvate carboxykinase (PEPCK) is well known as a key enzyme involved in the metabolic pathway of gluconeogenesis in organisms, but the information about its involvement in immune response is still very limited. In the present study, a novel PEPCK homolog named CgPEPCK was identified from oyster Crassostrea gigas.
Zhao Lv +9 more
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Phosphoenolpyruvate carboxykinase (PEPCK) is well known as a key enzyme involved in the metabolic pathway of gluconeogenesis in organisms, but the information about its involvement in immune response is still very limited. In the present study, a novel PEPCK homolog named CgPEPCK was identified from oyster Crassostrea gigas.
Zhao Lv +9 more
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Regulation of phosphoenolpyruvate carboxykinase (GTP) synthesis in the kidney.
Current problems in clinical biochemistry, 1978Phosphoenolpyruvate carboxykinase activity increases in the kidney after glucocorticoid administration and in acidosis. In both cases, a selective stimulation of the synthesis of phosphoenolpyurvate carboxykinase can account for the augmentation of the enzyme level.
P B, Iynedjian, R W, Hanson
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European Journal of Biochemistry, 1978
The mRNA coding for the gluconeogenic enzyme phosphoenolpyruvate carboxykinase (GTP) (EC 4.1.1.32) was partially purified from the liver of cyclic-AMP-treated rats by a procedure involving multiple oligo(dT)-cellulose chromatographies and sucrose gradient fractionations.
P B, Iynedjian, R W, Hanson
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The mRNA coding for the gluconeogenic enzyme phosphoenolpyruvate carboxykinase (GTP) (EC 4.1.1.32) was partially purified from the liver of cyclic-AMP-treated rats by a procedure involving multiple oligo(dT)-cellulose chromatographies and sucrose gradient fractionations.
P B, Iynedjian, R W, Hanson
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Somatic Cell and Molecular Genetics, 1985
The structural gene Pck-1, encoding cytosolic phosphoenolpyruvate carboxykinase (GTP) (PEPCK; EC 4.1.1.32), has been assigned to mouse chromosome 2. This assignment was made based on genomic Southern transfer of rat-mouse and hamster-mouse hybrid DNAs using a rat kidney cloned cDNA of the PEPCK gene as a probe. Conclusive evidence for the cosegregation
J, Lem, R E, Fournier
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The structural gene Pck-1, encoding cytosolic phosphoenolpyruvate carboxykinase (GTP) (PEPCK; EC 4.1.1.32), has been assigned to mouse chromosome 2. This assignment was made based on genomic Southern transfer of rat-mouse and hamster-mouse hybrid DNAs using a rat kidney cloned cDNA of the PEPCK gene as a probe. Conclusive evidence for the cosegregation
J, Lem, R E, Fournier
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Biochemistry, 1985
Using an in vitro assay with isolated rat nuclei, we have determined that thyroid hormone causes a 4-6-fold increase in the synthesis of mRNA coding for phosphoenolpyruvate carboxykinase. Proportional changes were seen in the steady-state cytosolic mRNA levels for phosphoenolpyruvate carboxykinase.
D S, Loose +3 more
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Using an in vitro assay with isolated rat nuclei, we have determined that thyroid hormone causes a 4-6-fold increase in the synthesis of mRNA coding for phosphoenolpyruvate carboxykinase. Proportional changes were seen in the steady-state cytosolic mRNA levels for phosphoenolpyruvate carboxykinase.
D S, Loose +3 more
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