Results 171 to 180 of about 19,538 (222)
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Glutaminase in human platelets
Clinica Chimica Acta, 1983Summary The activity of phosphate activated glutaminase, which is the major enzyme yielding glutamate from glutamine has been measured in human blood platelets. The enzyme shows good reproducibility in split duplicate assays and is stable over time. Platelets retain more enzyme activity when stored at 4°C in a buffered medium than when stored frozen.
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MODULATORS OF GLUTAMINASE ACTIVITY
Journal of Neurochemistry, 1972Abstract— The activating effect of GTP on particulate preparations of glutaminase from rat brain or rat kidney was competitively inhibited by cyclic guanosine 3′,5′‐monophosphate (c‐GMP). Similarly, the effect of ATP was inhibited by cyclic adenosine 3′,5′‐monophosphate (c‐AMP). In the absence of an added activator, the glutaminase activity of brain or
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Mammalian glutaminase isozymes in brain
Metabolic Brain Disease, 2012Glutamine/glutamate homeostasis must be exquisitely regulated in mammalian brain and glutaminase (GA, E.C. 3.5.1.2) is one of the main enzymes involved. The products of GA reaction, glutamate and ammonia, are essential metabolites for energy and biosynthetic purposes but they are also hazardous compounds at concentrations beyond their normal ...
Javier, Márquez +6 more
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Hormonal control of hepatic glutaminase
Advances in Enzyme Regulation, 1995(1) Glucagon activates hepatic glutaminase in vivo. Mitochondria from glucagon-injected rats retain an enhanced capacity to catabolize glutamine and this is more sensitive to activation by inorganic phosphate. The glucagon-elicited stimulation of glutaminase is not evident in broken mitochondria.
J T, Brosnan, H S, Ewart, S A, Squires
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On glutaminase activity in mammalian synaptosomes
Brain Research, 1976A large proportion (30%) of tissue glutaminase activity was found localized in synaptosome fractions as well as purified mitochondrial fractions, where it is also enriched on a protein basis (2-fold). Sulphate was more effective (2-8-fold) than phosphate or chloride in activating the enzyme at concentrations above 10-12 mM, but equivalent to phosphate ...
H F, Bradford, H K, Ward
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Hepatic glutaminase expression: relationship to kidney‐type glutaminase and to the urea cycle
The FASEB Journal, 1993Glutamine functions as a major transport form of nitrogen and carbon within the body. In the liver, glutamine is hydrolyzed by a unique liver‐type, phosphate‐activated glutaminase, and the end products of hepatic glutamine catabolism are glucose and urea. Other tissues possess a different, kidney‐type, glutaminase isozyme.
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The activity of glutaminase in the human placenta
Archives of Biochemistry and Biophysics, 1951Abstract Homogenates and extracts of human placenta are able to desamidate glutamine by means of an enzyme which has the properties of glutaminase. Placental glutaminase is activated by phosphate. Its pH optimum lies at 9.0. A method for its assay in placental homogenate is described.
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