Results 191 to 200 of about 41,991 (249)

Mitochondrial phosphoenolpyruvate carboxykinase deficiency

European Journal of Pediatrics, 1986
A 3-month-old girl presented with anorexia, failure to thrive and drowsiness. She was mildly icteric with hepatomegaly and peripheral oedema. Disordered liver function tests were associated with the biopsy appearances of a giant cell hepatitis and with a Fanconi syndrome. At the age of 16 weeks she collapsed with profound hypoglycaemia.
J V, Leonard, K, Hyland, N, Furukawa, P T, Clayton   +3 more
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Phosphoenolpyruvate carboxykinase activity in invertebrates

Comparative Biochemistry and Physiology, 1964
Abstract 1. 1. The presence of P-enolpyruvate carboxykinase has been demonstrated in nine species of molluscs and one species of coelenterate. In most, the activity was considerably higher than in rat liver and in some of them the activity was much higher than in chicken liver. 2. 2.
J W, SIMPSON, J, AWAPARA
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TWO CASES OF PHOSPHOENOLPYRUVATE CARBOXYKINASE DEFICIENCY

Acta Paediatrica, 1976
ABSTRACT. Two children are described who suffered from hypoglycemia and liver impairment. Assays of gluconeogenic enzymes in liver samples taken immediately after death demonstrated a deficiency of phosphoenolpyruvate carboxykinase, a key enzyme of gluconeogenesis.
Hommes, F A, Bendien, K, Elema, J D, Bremer, H J, Lombeck, I   +4 more
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Regulation of Gluconeogenesis at Phosphoenolpyruvate Carboxykinase

1984
Publisher Summary This chapter discusses the regulation of gluconeogenesis at phosphoenolpyruvate carboxykinase. It describes the formation of phosphoenolpyruvate (P-enolpyruvate) from oxalacetate. P-enolpyruvate carboxy-kinase (PEPCK) has only a single known function but it exists in two isozyme forms in two different cellular locations and its ...
H, Lardy, P E, Hughes
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The kinetic mechanism of yeast phosphoenolpyruvate carboxykinase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1993
The kinetic mechanism of yeast phosphoenolpyruvate carboxykinase, in the physiological direction, has been determined. Product inhibition using KHCO3 showed competitive inhibition, when both oxalacetate (OAA) and ATP were varied. Phosphoenolpyruvate showed noncompetitive inhibition against OAA, and competitive inhibition with respect to ATP. Conversely,
A M, Jabalquinto, E, Cardemil
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Inactivation of phosphoenolpyruvate carboxykinase by acetaldehyde

Biochemical and Biophysical Research Communications, 1976
Abstract 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.
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Regulation and roles of phosphoenolpyruvate carboxykinase in plants

Archives of Biochemistry and Biophysics, 2003
Phosphoenolpyruvate 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.
Richard C, Leegood, Robert P, Walker
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Phosphoenolpyruvate carboxykinase activity in human liver

Forensic Science International, 1986
The 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
C A, McGraw, G F, Vawter, G, Hug
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Phosphoenolpyruvate carboxykinase from Fasciola hepatica

International Journal for Parasitology, 1982
Abstract 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.
C A, Behm, C, Bryant
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Electrophoretic and chromatographic separation of phosphoenolpyruvate carboxykinases

Biochimica et Biophysica Acta (BBA) - Enzymology, 1971
Abstract 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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