Results 251 to 260 of about 41,691 (279)
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The Plant Journal, 2012
Malate, along with potassium and chloride ions, is an important solute for maintaining turgor pressure during stomatal opening. Although malate is exported from guard cells during stomatal closure, there is controversy as to whether malate is also ...
S. Penfield+6 more
semanticscholar +1 more source
Malate, along with potassium and chloride ions, is an important solute for maintaining turgor pressure during stomatal opening. Although malate is exported from guard cells during stomatal closure, there is controversy as to whether malate is also ...
S. Penfield+6 more
semanticscholar +1 more source
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
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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
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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.
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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
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Limited proteolysis ofSaccharomyces cerevisiae phosphoenolpyruvate carboxykinase
Journal of Protein Chemistry, 1993Incubation of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase with trypsin under native conditions cases a time-dependent loss of activity and the production of protein fragments. Cleavage sites determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis and sequence analyses identified protease-sensitive peptide bonds between ...
Ana María Jabalquinto+3 more
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Ochratoxin A, an in vivo inhibitor of renal phosphoenolpyruvate carboxykinase
Archives of Biochemistry and Biophysics, 1981Abstract Ochratoxin A, a nephrotoxin produced as a secondary metabolite by A. ochraceus, is a potent inhibitor of renal PEPCK activity, in vivo. When fed orally to rats for 2 days, renal PEPCK activity is reduced 50% by a total dose of 0.3-0.5 mg toxin. Renal gluconeogenic capacity is reduced only after PEPCK activity is inhibited by 50%.
Herman Meisner, Patricia Meisner
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Insulin Regulates Expression of the Phosphoenolpyruvate Carboxykinase Gene
1986Publisher Summary This chapter describes insulin regulates expression of the phosphoenolpyruvate carboxykinase (PEPCK) gene. The inhibitory effect of insulin on PEPCK gene transcription is (1) achieved at physiologic concentrations of the hormone, (2) mediated through the insulin receptor, (3) specific, (4) seen in the absence of on-going protein ...
Daryl K. Granner+3 more
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Phosphoenolpyruvate carboxykinase and gluconeogenesis in cotyledons of Cucurbita pepo
Biochimica et Biophysica Acta (BBA) - Enzymology, 19781. The aim of this work was to investigate the role of phosphoenolpyruvate carboxykinase (ATP:oxaloacetate carboxy-lyase (transphosphorylating) EC 4.1.1.49) in the conversion of fat to sugar by the cotyledons of seedlings of Cucurbita pepo. 2. The enzyme was partially purified from the cotyledons of 5-day-old seedlings.
T. ap Rees, Richard C. Leegood
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