Results 181 to 190 of about 27,569 (215)

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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Glutaminase Activity and Neocortical Excitability

Nature, 1965
THE work recorded here was carried out in order to ascertain whether glutaminase I activity in the neocortex of the cat plays a part in the glutamate-glutamine system changes induced by the appearance and development of an epileptogenic focus produced by application of mescaline1.
N, Mison-Crighel, C, Pintilie, E, Crighel   +2 more
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Safety evaluation of yeast glutaminase

Food and Chemical Toxicology, 2000
The consumption of soy and soy products (including soy sauce) has been increasing in Western countries due to purported health benefits of soy (cancer protective, estrogenic effects). In addition to providing soy proteins and isoflavones, soy sauce also functions as a flavor enhancer and is able to impart a "umami" taste.
K, Ohshita, Y, Nakajima, J, Yamakoshi, S, Kataoka, M, Kikuchi, M W, Pariza   +5 more
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Glutaminase isozymes in rat kidney

Biochemical and Biophysical Research Communications, 1966
Abstract In 1958 Sayer and Roberts reported on the mode of activation of glutaminase by phosphate using a dog kidney preparation. More recently Kvamme et al. (1965) showed that the activation by phosphate involves a conformational change of the enzyme protein of pig kidney. The authors found that there are two types of glutaminase in rat kidney.
N, Katunuma, I, Tomino, H, Nishino
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MODULATORS OF GLUTAMINASE ACTIVITY

Journal of Neurochemistry, 1972
Abstract— 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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Endotoxin Stimulates Lymphocyte Glutaminase Expression

Archives of Surgery, 1993
Glutamine is the principal fuel used by lymphocytes. It is hydrolyzed by the glutaminase enzyme, which regulates the rate of intracellular glutamine metabolism. Since lymphocyte glutamine utilization is increased during infection to support cellular proliferation, we hypothesized that endotoxin regulates lymphocyte glutaminase expression at the ...
P, Sarantos, K, Ockert, W W, Souba
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Glutaminase in human platelets

Clinica Chimica Acta, 1983
Summary 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, 2018
The 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, LiXia, Chen, Sanshan, Jin, Hua, Li   +3 more
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Pig renal glutaminase—Another view

Journal of Molecular Biology, 1973
Abstract 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, 1971
AbstractPig 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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