Search results for "Rana esculenta"

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Pericardium of the frog, Rana esculenta, is morphologically designed as a lymphatic space

2003

The importance of the pericardium and the pericardial fluid (PF) in the control of cardiac function has emerged over the past few years. Despite the acknowledgment that amphibians are exposed to both dehydration and excessive water accumulation, nothing is known about their pericardial structure and the morphological basis of the PF formation. We have studied the parietal pericardium (PP) morphology in Rana esculenta by electron microscopy. SEM images of the inner surface, which lines the pericardial cavity, revealed the presence of large vesicles and many small circular openings. TEM observations showed that the PP is made up of an inner mesothelial lining, often constituted by two layers …

AnimalAngiotensin IIRana esculentaAgricultural and Biological Sciences (miscellaneous)Lymphatic SystemMicroscopy ElectronAngiotensin II; Fluid transfer; Pericardial mesothelium; Rana esculenta; Angiotensin II; Animals; Endocrine Glands; Lymphatic System; Microscopy Electron; Pericardium; Rana esculenta; Agricultural and Biological Sciences (miscellaneous); Developmental Biology; AnatomyEndocrine GlandsAnimalsFluid transferPericardial mesotheliumAnatomyPericardiumEndocrine GlandDevelopmental Biology
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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase from frog skeletal muscle: purification, kinetics and immunological properties.

1993

Fructose 2,6-bisphosphate is the most potent activator of 6-phosphofructo-1-kinase, a key regulatory enzyme of glycolysis in animal tissues. This study was prompted by the finding that the content of fructose 2,6-bisphosphate in frog skeletal muscle was dramatically increased at the initiation of exercise and was closely correlated with the glycolytic flux during exercise. 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, the enzyme system catalyzing the synthesis and degradation of fructose 2,6-bisphosphate, was purified from frog (Rana esculenta) skeletal muscle and its properties were compared with those of the rat muscle type enzyme expressed in Escherichia coli using recombinant DN…

PhysiologyPhosphofructokinase-2BiologyBiochemistrychemistry.chemical_compoundEndocrinologymedicineFructosediphosphatesAnimalsGlycolysisPhosphorylationEcology Evolution Behavior and Systematicschemistry.chemical_classificationMolecular massImmunochemistryMusclesPhosphotransferasesSkeletal muscleRana esculentaFructoseHydrogen-Ion ConcentrationMolecular WeightKineticsmedicine.anatomical_structureEnzymechemistryFructose 26-bisphosphateBiochemistryGRENOUILLEAnimal Science and ZoologyPhosphoenolpyruvate carboxykinaseProtein KinasesJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology
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