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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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Glutaminase inhibitors: a patent review
Expert Opinion on Therapeutic Patents, 2018The kidney-type glutaminase (GLS) controlling the first step of glutamine metabolism is overexpressed in many cancer cells. Targeting inhibition of GLS shows obvious inhibitory effects on cancer cell proliferation. Therefore, extensive research and development of GLS inhibitors have been carried out in industrial and academic institutions over the past
CanRong, Wu +3 more
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Pig renal glutaminase—Another view
Journal of Molecular Biology, 1973Abstract Olsen et al. (1973) interpret their observations of pig renal glutaminase in terms of a conformationsl change in the dimers making up a polymer. It is argued here that the same data can be used to explain the same polymer structure without involving conformational changes, and a model is proposed to support this view.
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ACTIVATION OF PIG BRAIN GLUTAMINASE
Journal of Neurochemistry, 1971AbstractPig brain glutaminase (EC 3.5.1.2, l‐glutamine amidohydrolase) is activated by certain anions (e.g. phosphate, fluoride, carboxylic acids) and inhibited by others (e.g. chloride, bromide, iodide and glutamate). The only cation which has been found to activate the enzyme is the ammonium ion.
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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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[Characteristics of Triticale glutaminase].
Prikladnaia biokhimiia i mikrobiologiia, 2002The glutaminase (EC 3.5.1.2) isolated from seedlings of triticale (Triticale sp.) had a pH optimum of about 8, was inhibited with excess substrate (glutamine), and reaction products (glutamate and NH4+). A monovalent anion (Cl-) and a multivalent anion (phosphate) were shown to activate the glutaminase.
L I, Sidel'nikova +3 more
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