Results 121 to 130 of about 30,715 (166)
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Stabilization of mouse brain glutamic decarboxylase

Experientia, 1972
Le GAD du cerveau de souris, une enzyme sensible au SH, peut etre purifie en presence de 2-aminoethyl-isothiouronium-bromide (AET), une substance radioprotective. AET, qui existe en solution neutre, comme 2-mercaptoethyl guanidine, protege les enzymes qui contiennent le SH bien mieux que les quantites isomolares du GSH ou du dithioerythretol (Cleland's
E, Roberts, M, Szabo, B, Haber
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Immunoaffinity purification of l-glutamate decarboxylase

Neurochemistry International, 1990
A rapid and efficient immunoaffinity procedure for the purification of a new form of brain l-glutamate decarboxylase (GAD) is described. A well characterized monoclonal antibody against rat brain GAD is used as an affinity ligand. The GAD-anti-GAD complex is dissociated by a relatively gentle condition e.g. 0.2 M acetate buffer, pH 4 or 5.
J Y, Wu   +4 more
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Glutamate‐Dependent Active‐Site Labeling of Brain Glutamate Decarboxylase

Journal of Neurochemistry, 1990
AbstractA major regulatory feature of brain glutamate decarboxylase (GAD) is a cyclic reaction that controls the relative amounts of holoenzyme and apoenzyme [active and inactive GAD with and without bound pyridoxal 5′‐phosphate (pyridoxal‐P, the cofactor), respectively].
D L, Martin, S J, Wu, S B, Martin
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Irreversible inhibition of glutamate decarboxylase by .alpha.-(fluoromethyl)glutamic acid

Biochemistry, 1981
alpha-(Fluoromethyl)glutamic acid (FMG) was synthesized and shown to be an active site directed irreversible inhibitor of glutamate decarboxylase (EC 4.1.1.15) from Escherichia coli. The KI for the active enantiomer is 1.4 microM, and the kinh = 5.9 X 10(-3) s-1.
D, Kuo, R R, Rando
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Decarboxylases Brain Glutamate Decarboxylase as a Model

1983
Decarboxylases are a group of diverse enzymes that catalyze the decarboxylation of amino acids, keto acids, and others. They have been described in bacteria, plants, and animals.1,2 Although some of their functions remain unknown, it is clear that several of the decarboxylases have biosynthetic functions; e.g., ornithine and adenosylmethionine ...
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Glutamate decarboxylase. Inhibition by monocarboxylic acids

Archives of Biochemistry and Biophysics, 1972
Abstract Aliphatic monocarboxylic acids are demonstrated to be substrate competitive inhibitors of bacterial glutamate decarboxylase. A chain-length effect is observed in the inhibition by the monocarboxylic acids with n -valeric acid functioning as the most effective inhibitor.
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The application of glutamic acid α-decarboxylase for the valorization of glutamic acid

Green Chemistry, 2009
Glutamic acid is an important constituent of waste streams from biofuels production. It is an interesting starting material for the synthesis of nitrogen containing bulk chemicals, thereby decreasing the dependency on fossil fuels. On the pathway from glutamic acid to a range of molecules, the decarboxylation of glutamic acid to γ-aminobutyric acid ...
Lammens, T.M.   +4 more
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Glutamic acid decarboxylase antibodies in Satoyoshi syndrome

Annals of Neurology, 2004
Contains fulltext : 58378.pdf (Publisher’s version ) (Closed access)
Drost, G.   +3 more
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Brain Glutamate Decarboxylase

2003
Glutamate decarboxylase (glutamate 1-carboxylyase, EC 4.1.1.15, GAD)* IS the major, rate-limiting enzyme in brain for synthesizing gamma-aminobutyric acid (GABA). Total GAD activity in brain is 10-20 times greater than the observed rate of GABA synthesis (Collins, 1972; Matsui and Deguchi, 1977; Casu and Gale, 1981), indicating that GAD operates at ...
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Regulatory properties of brain glutamate decarboxylase

Cellular and Molecular Neurobiology, 1987
1. Glutamate decarboxylase is a focal point for controlling gamma-aminobutyric acid (GABA) synthesis in brain. Several factors that appear to be important in the regulation of GABA synthesis have been identified by relating studies of purified glutamate decarboxylase to conditions in vivo. 2. The interaction of glutamate decarboxylase with its cofactor,
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