Results 221 to 230 of about 227,873 (271)

Radioimmunoassay for Glutamic Acid Decarboxylase-65

Diabetes Technology & Therapeutics, 1999
Glutamic acid decarboxylase-65 (GAD65), the enzyme that catalyzes the formation of gamma-aminobutyric acid (GABA), is the major autoantigen in both type 1 (insulin-dependent) diabetes and stiff-man syndrome (SMS). The observation that GAD65 autoantibodies may be present for years before the clinical onset of diabetes raises the question of when GAD65 ...
W, Hao, T, Daniels, D G, Pipeleers, A, Smismans, H, Reijonen, G T, Nepom, A, Lernmark   +6 more
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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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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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Food-grade γ-aminobutyric acid production by immobilized glutamate decarboxylase from Lactobacillus plantarum in rice vinegar and monosodium glutamate system

Biotechnology Letters, 2021
L. Yao, J. Cao, C. Lyu, F. Fan, H. Wang, H. Cao, J. Huang, L. Mei   +7 more
semanticscholar   +1 more source

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 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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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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