Results 191 to 200 of about 43,118 (240)

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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Circular dichroism of L-glutamic acid decarboxylase

Biochemical and Biophysical Research Communications, 1967
Shukuya and Schwert (1960a) have shown that L-ylutamic acid decarboxylase (GAD) from E_. coli exhibits a sharply pHdependen,t reversible spectral change centered at pH 5.6. At pH's less than 5, the enzyme has an absorbance peak at 415 mp, while at pH's greater than 6, this peak is replaced by one at 340 mu.
T E, Huntley, D E, Metzler
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Glutamic acid decarboxylase autoantibodies and neurological disorders

Neurological Sciences, 2002
Glutamic acid decarboxylase (GAD) is the enzyme that catalyses the production of GABA, a major neurotransmitter of the central nervous system. Antibodies to GAD (GAD-Ab) were first recognised in a patient affected by stiff-person syndrome; subsequently they were reported in a large number of cases with type 1 diabetes.
Vianello M, Tavolato B, Giometto B
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Encephalitis associated with glutamic acid decarboxylase autoantibodies

Neurology, 2001
Antiglutamic acid decarboxylase (GAD-A) autoantibodies were originally reported in patients with stiff-man syndrome (SMS).1 Successive studies have shown that GAD-A was implicated in the pathogenesis of type 1 diabetes.2 High titers of GAD-A were recently reported in neurologic patients with disorders other than SMS, in particular ataxia3,4⇓ and ...
Marchiori GC, Vaglia A, Vianello M, Bardin PG, Giometto B   +4 more
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Cerebellar ataxia with glutamic acid decarboxylase autoantibodies

Neurology, 1999
Degenerative cerebellar ataxia with autoantibodies against glutamic acid decarboxylase (GAD) is a rare disorder and may represent a subset of ataxias previously classified as idiopathic. The authors report a patient with progressive cerebellar ataxia, insulin-dependent diabetes mellitus, and GAD antibodies who responded to i.v. immunoglobulins.
M, Abele, M, Weller, S, Mescheriakov, K, Bürk, J, Dichgans, T, Klockgether   +5 more
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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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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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Spectrophotometric assay of l-glutamic acid decarboxylase

Analytical Biochemistry, 1970
Abstract A spectrophotometric method has been developed for the measurement of glutamic acid decarboxylase activity and applied to the kinetic study of the enzyme from Clostridium perfringens . The results are compared with those obtained by manometric method.
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