Results 231 to 240 of about 28,180 (258)
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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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A mitochondrial phosphoenolpyruvate carboxykinase from rat brain
Archives of Biochemistry and Biophysics, 1972Phosphoenolpyruvate carboxykinase from the rat brain has been purified approximately 6000-fold. This purified enzyme was stable at −20 °C for several months. Phosphoenolpyruvate carboxykinase from the rat brain was found to be mitochondrial, in contrast to that in the rat liver where this enzyme was always present in the soluble form.
R.H.C. Cheng, S.-C. Cheng
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Phosphoenolpyruvate carboxykinase (ATP) [PDF]
, 1990 Margit Salzmann, Dietmar Schomburg
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Phosphoenolpyruvate carboxykinase: Structure, function and regulation
2002Abstract The aim of this article is to outline our understanding of the enzyme phosphoenolpyruvate carboxykinase (PEPCK). Although emphasis is placed on the enzyme derived from flowering plants, other organisms are also considered, because comparative studies provide invaluable information. The following points are considered in detail.
Robert P. Walker, Zhi-Hui Chen
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Phosphoenolpyruvate carboxykinase activity in Ascaris suum muscle
Comparative Biochemistry and Physiology, 1969Abstract 1. 1. Phosphoenolpyruvate (PEP) carboxykinase activity was measured for four subcellular fractions of Ascaris suum muslce. Mos activity was associated with the soluble fraction. 2. 2. The reaction had a pH optimum of about 7·2. 3. 3. Mn ++ was a more effective promoter of the reaction than Mg ++ . 4. 4.
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The Regulation of Phosphoenolpyruvate Carboxykinase in Fetal Rat Liver [PDF]
Enzyme and Protein, 1973 Lea Reshef +3 more
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Phosphoenolpyruvate Carboxykinase in the Developing Pig Liver
Neonatology, 1971M. Cornblath, K.R. Swiatek, J.T. Tildon
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Phosphoenolpyruvate carboxykinase (pyrophosphate)
1990Dietmar Schomburg, Margit Salzmann
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