Results 221 to 230 of about 26,859 (247)
Some of the next articles are maybe not open access.
Regulation and roles of phosphoenolpyruvate carboxykinase in plants
Archives of Biochemistry and Biophysics, 2003Phosphoenolpyruvate carboxykinase (PCK) is probably ubiquitous in flowering plants, but is confined to certain cells or tissues. It is regulated by phosphorylation, which renders it less active by altering both its substrate affinities and its sensitivity to regulation by adenylates.
Robert P. Walker, Richard C. Leegood
openaire +2 more sources
Inactivation of phosphoenolpyruvate carboxykinase by acetaldehyde
Biochemical and Biophysical Research Communications, 1976Abstract Preincubation with acetaldehyde at 37°C inactivates rat liver phosphoenolpyruvate carboxykinase. The inactivation is dependent upon the acetaldehyde concentration and the pH and duration of preincubation, and is prevented but not reversed by glutathione.
openaire +3 more sources
Phosphoenolpyruvate carboxykinase activity in human liver
Forensic Science International, 1986The activity of phosphoenolpyruvate carboxykinase (EC 4.1.1.32) (PEPCK), a rate-limiting gluconeogenic enzyme, was found decreased by others in genetically determined disorders and in Sudden Infant Death Syndrome (SIDS). To understand these findings, we made a systematic study of normal human hepatic PEPCK activities in specimens obtained under various
Gordon F. Vawter +2 more
openaire +3 more sources
Phosphoenolpyruvate carboxykinase from Fasciola hepatica
International Journal for Parasitology, 1982Abstract Behm C. A. and Bryant C. 1982. Phosphoenolpyruvate carboxykinase from Fasciola hepatica. International Journal for Parasitology 12 : 271–278. The kinetic properties of a partially purified preparation of phosphoenolpyruvate carboxykinase (PEPCK) from F. hepatica were examined.
Carolyn A. Behm, Christopher Bryant
openaire +3 more sources
Regulation of phosphoenolpyruvate carboxykinase (GTP) gene transcription
Molecular and Cellular Biochemistry, 1991Transcription of the gene for phosphoenolpyruvate carboxykinase is regulated by several hormones which control the level of glucose synthesis in vertebrate animals. A 490 bp segment located at the 5' end of the structural gene contains the necessary regulatory elements to account for the pattern of transcriptional regulation characteristic of the ...
Jinsong Liu, R. W. Hanson
openaire +3 more sources
Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1976Various analogues of adenosine 5'-diphosphate with modifications in the heterocyclic base residue were tested as substrates of rabbit muscle pyruvate kinase (ATP:pyruvate 2-O-phosphotransferase, EC. 2.7.1.40) and guinea pig liver mitochondrial phosphoenolpyruvate carboxykinase (GTP:oxaloacetate carboxy-lyase (transphosphorylating), EC 4.1.1.32).
Bârzu, O. +8 more
openaire +4 more sources
REGULATION OF PHOSPHOENOLPYRUVATE CARBOXYKINASE (GTP) GENE EXPRESSION
Annual Review of Biochemistry, 1997Phosphoenolpyruvate carboxykinase (GTP) (EC 4.1.1.32) (PEPCK) is a key enzyme in the synthesis of glucose in the liver and kidney and of glyceride-glycerol in white adipose tissue and the small intestine. The gene for the cytosolic form of PEPCK (PEPCK-C) is acutely regulated by a variety of dietary and hormonal signals, which result in alteration of ...
Lea Reshef, Richard W. Hanson
openaire +2 more sources
Electrophoretic and chromatographic separation of phosphoenolpyruvate carboxykinases
Biochimica et Biophysica Acta (BBA) - Enzymology, 1971Abstract Electrophoresis of phosphoenolpyruvate carboxykinases on acrylamide gel gives marked separation between the cytosol enzyme from rat liver and the mitochondrial enzyme from chicken liver. These enzymes are also resolved on hydroxyapatite chromatography as are the mitochondrial and cytosol enzymes from sheep liver.
openaire +3 more sources
Analogs of oxalacetate as potential substrates for phosphoenolpyruvate carboxykinase
Archives of Biochemistry and Biophysics, 1990Structural analogs of the substrate oxalacetate were examined as potential substrates and inhibitors for chicken liver mitochondrial phosphoenolpyruvate (P-enolpyruvate) carboxykinase. Steady-state kinetics were employed to characterize the inhibitory effects of these substrate analogs with the enzyme.
Peter F. Guidinger, Thomas Nowak
openaire +3 more sources
Phosphoenolpyruvate carboxykinase is a nuclear enzyme in rats and chickens
International Journal of Biochemistry, 1983The presence of phosphoenolpyruvate carboxykinase (PEPCK) in the nuclei of chicken liver cells was confirmed using two experimental designs. PEPCK was found to be enriched in the nuclear fraction of rat liver, a species whose hepatic PEPCK is reported to be predominantly cytosolic.
Gene R. Herzberg +2 more
openaire +3 more sources