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Regional-specific GABAergic imbalance in cisplatin-induced neuropathy and antiallodynic effects of intraplantar baclofen in rats. [PDF]

Sci Rep
Quan Y, Zhang E, Nan Y, Lin H.
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Glutamic Acid Decarboxylase Antibody

2014
Glutamic acid decarboxylase (GAD) catalyzes the conversion of glutamic acid into gamma-amino butyric acid within pancreatic islet β cells. Autoantibodies against GAD (GADA) are found in patients with type 1 diabetes mellitus (T1DM), stiff-person syndrome, and epilepsy.
C. Crotti, C. Selmi
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Glutamate decarboxylase in bacteria.

2017
gamma -Aminobutyrate (GABA) is a non-proteinaceous amino acid which plays different roles in the living systems. GABA is biochemically produced by the irreversible a-decarboxylation of l-glutamate catalysed by glutamate decarboxylase (Gad), a widespread enzyme distributed among eukaryotes and prokaryotes. Structural features of the plant, mammalian and
GIOVANNERCOLE, FABIO, PENNACCHIETTI, Eugenia, DE BIASE, Daniela   +2 more
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Inactivation of glutamate decarboxylase by bromopyruvate

Biochemical and Biophysical Research Communications, 1974
Abstract Bromopyruvate was shown to inhibit E. coli glutamate decarboxylase competitively with respect to L-glutamate. High concentrations of bromopyruvate caused a time-dependent inactivation of glutamate decarboxylase. However, the apoenzyme was rapidly and irreversibly inactivated by bromopyruvate with an inactivation constant of 490 1 mole ...
M L, Fonda, R F, DeGrella
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Plasma glutamate decarboxylase activity in neuropsychiatry

Psychiatry Research, 1982
Plasma glutamate decarboxylase (GAD) activity was measured in patients with endogenous psychoses and neurologic diseases. Unmedicated schizophrenic patients showed no difference in plasma GAD levels compared to controls. Administration of neuroleptics together with anticholinergic agents increased plasma GAD activity in schizophrenic patients. Compared
H, Kaiya, M, Namba, H, Yoshida, S, Nakamura   +3 more
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L-Glutamate Decarboxylase

1979
Much progress has been made in recent years regarding enzymological aspects of mammalian brain GAD, such as its purification and characterization, but some uncertainty still remains concerning its molecular weight and forms, and its subunit structure.
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Borohydride reduction of l-glutamate decarboxylase

Archives of Biochemistry and Biophysics, 1965
Abstract l -Glutamate decarboxylase was purified from a sucrose-negative strain of Escherichia coli . The specific activity of 60% pure enzyme was 19,550 μl/10 minutes/mg. Borohydride reduction at pH 4.8–5.2 resulted in (a) the disappearance of the peak at 415 mμ, and appearance of an inflection at 330 mμ; (b) loss of 97% of the activity; (c ...
J A, ANDERSON, H F, CHANG
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Two genes encode distinct glutamate decarboxylases

Neuron, 1991
gamma-Aminobutyric acid (GABA) is the most widely distributed known inhibitory neurotransmitter in the vertebrate brain. GABA also serves regulatory and trophic roles in several other organs, including the pancreas. The brain contains two forms of the GABA synthetic enzyme glutamate decarboxylase (GAD), which differ in molecular size, amino acid ...
M G, Erlander, N J, Tillakaratne, S, Feldblum, N, Patel, A J, Tobin   +4 more
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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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