Results 321 to 330 of about 358,941 (349)
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Isocitric Lyase and Isocitric Dehydrogenase in Germinating Lettuce

Physiologia Plantarum, 1968
AbstractA soluble isocitric lyase is shown to occur in lettuce seeds. Its activity increases during germination till 72 hours and then falls again. No particulate lyase could be detected. In addition both a soluble and a particulate isocitric dehydrogenase is present in the seeds. Both enzymes react with NAD as well as with NADP.
A. M. Mayer   +2 more
openaire   +1 more source

The estimation of d-isocitric acid in urine using isocitrate dehydrogenase

Clinica Chimica Acta, 1978
The amount of D-isocitric acid in urine has been estimated using the enzyme isocitrate dehydrogenase. The technique is rapid and easy to perform. Reproducibility of results was good and results from recovery experiments were excellent. The concentration range for early morning urine samples from normal adults was 0.08-0.65 mmol/l with a mean of 0.29 ...
D J, Sutor, J M, Percival
openaire   +2 more sources

Mitochondrial Isocitrate Dehydrogenase and Isocitrate Oxidation of Rat Ventral Prostate

Enzyme, 1976
Mitochondrial preparations isolated from rat ventral prostate were capable of oxidizing isocitrate by way of NADP isocitrate dehydrogenase (NADP-IDH) and NAD-IDH. NAD-IDH activity required ADP for activation. The pH responses for NAD-IDH and NADP-IDH were quite different.
L C, Costello, R, Franklin, R, Stacey
openaire   +2 more sources

Isocitrate dehydrogenase 1 mutations in melanoma frequently co‐occur with NRAS mutations

Histopathology, 2018
Isocitrate dehydrogenase 1 (IDH1) is a metabolic enzyme that converts isocitrate to α‐ketoglutarate. IDH1 mutations are associated with the accumulation of the oncometabolite D‐2‐hydroxyglutarate, which acts as an epigenetic modifier, and the development
K. Linos, L. Tafe
semanticscholar   +1 more source

The inactivation of isocitrate dehydrogenase by a lipid peroxide

Archives of Biochemistry and Biophysics, 1971
Abstract The isocitrate dehydrogenases of rat liver were found extremely sensitive to inacvation by linoleic acid hydroperoxide. Lipid peroxide was much more effective than other peroxides and sulfhydryl reagents tested. Dehydrogenase activity of crude subcellular fractions was more sensitive than the activity of the purified enzyme. The inactivation
R C, Green, C, Little, P J, O'Brien
openaire   +2 more sources

Development of Novel Therapeutics Targeting Isocitrate Dehydrogenase Mutations in Cancer.

Current Topics in Medicinal Chemistry, 2018
Isocitrate dehydrogenases 1 and 2 (IDH1 and IDH2) are key metabolic enzymes that catalyze the conversion of isocitrate to α-ketoglutarate (αKG). IDH1 and IDH2 regulate several cellular processes, including oxidative respiration, glutamine metabolism ...
H. Sharma
semanticscholar   +1 more source

An Evaluation of Isocitric Dehydrogenase in Liver Disease

Annals of Internal Medicine, 1961
Excerpt Laboratory evaluation of hepatocellular damage has been aided in recent years by the development of new methods for measuring serum activities of enzymes released from injured liver cells.
N N, COHEN, H P, POTTER, G N, BOWERS
openaire   +2 more sources

Genetic polymorphism of Isocitrate dehydrogenase in Primates

Human Genetics, 1973
The genetic polymorphism of isocitrate dehydrogenase has been investigated in 400 Primates. Six different phenotypes of the soluble enzyme were demonstrated. The mitochondrial enzyme exhibited a uniform electrophoretic pattern.
J, Schmitt, H, Ritter
openaire   +2 more sources

Crystallization of NADP-Specific Isocitrate Dehydrogenase

Science, 1973
The first crystalline preparation of isocitrate dehydrogenase specific for nicotinamide adenine dinucleotide phosphate has been obtained with enzyme isolated from Escherichia coli . Scanning electron microscopy was employed to elucidate the structure of the crystals, which were found to exist as regular octahedrons ...
W F, Burke, J R, Swafford, H C, Reeves
openaire   +2 more sources

The regulatory properties of isocitrate dehydrogenase kinase and isocitrate dehydrogenase phosphatase from Escherichia coli ML308 and the roles of these activities in the control of isocitrate dehydrogenase

European Journal of Biochemistry, 1984
Isocitrate dehydrogenase kinase can use ATP but not other nucleoside triphosphates as a phosphate donor. It responds hyperbolically to both ATP and isocitrate dehydrogenase. The kinase is inhibited sigmoidally by low concentrations of DL‐isocitrate and hyperbolically by ADP, AMP, NADPH, phosphoenolpyruvate and several other effectors.
G A, Nimmo, H G, Nimmo
openaire   +2 more sources

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