Results 201 to 210 of about 56,211 (247)

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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Coenzyme binding site of glutamate decarboxylase

Biochemistry, 1980
Dissociation constants have been measured for the binding of a variety of simple analogues of pyridoxal 5'-phosphate to apoglutamate decarboxylase. Compounds studied have a simple alkyl or aryl group and a negatively charged substituent (phosphate, phosphonate, phosphoramidate, sulfate, sulfonate, or carboxylate).
M H, O'Leary, S W, Koontz
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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, J Y, Liu, C T, Lin, D, Evans, W H, Tsai   +4 more
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Glutamic acid decarboxylase in Mycobacterium leprae

Archives of Microbiology, 1983
Suspensions of Mycobacterium leprae purified from the organs (mostly spleen) of experimentally-infected armadillos (Dasypus novemcinctus, Linn) decarboxylated 1-(14C) glutamic acid liberating 14CO2. The reaction was pyridoxal phosphate-dependent and was inhibited by hydroxylamine, suggesting that it is a true amino acid decarboxylase.
K, Prabhakaran, E B, Harris, W F, Kirchheimer   +2 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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Inhibitors of crayfish glutamic acid decarboxylase

Neurochemical Research, 1984
Crayfish glutamic acid decarboxylase (GAD), like the homologous enzymes from other species, is inhibited by carbonyl-trapping agents (e.g. aminooxyacetic acid; AOAA) and sulfhydryl reagents (e.g. 5,5'-dithiobis-(2-nitrobenzoic acid); DTNB). It also is inhibited by the product GABA, many anions (e.g. SCN- and Cl-), and some cations (e.g. Zn+2).
R M, Grossfeld, S W, Yancey, C F, Baxter
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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., Verrips, A., Hooijkaas, H., Zwarts, M.J.   +3 more
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Structure and function ofl-glutamate decarboxylase

Neurochemical Research, 1991
Membrane bound L-glutamate decarboxylase (GAD) has been solubilized and partially purified from hog brain. The solubilized GAD appears to exist in two forms, alpha and beta, differing in their size and electrophoretic mobility. The alpha form has similar mobility as that of the soluble GAD in 7.5% and 5-25% gradient polyacrylamide gel electrophoresis ...
J Y, Wu, W M, Huang, L, Reed-Fourquet, J, Bao, B, Nathan, E, Wu, W H, Tsai   +6 more
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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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Effect of phosphonic analogues of glutamic acid on glutamate decarboxylase

Experientia, 1985
Among the phosphonic analogues of glutamic acid, only 4-amino-4-phosphono butyric acid, the compound which shows the highest affinity for pyridoxal phosphate, inhibits competitively both Escherichia coli and rat brain glutamate decarboxylases. Phosphinothricin, 2-amino-4-(methylphosphino)butyric acid, is a strong inhibitor of the mammalian enzyme.
A M, Lacoste, S, Mansour, A, Cassaigne, E, Neuzil   +3 more
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