Results 211 to 220 of about 227,873 (271)

Screening of gamma‐aminobutyric acid‐producing lactic acid bacteria and the characteristic of glutamate decarboxylase from Levilactobacillus brevis F109‐MD3 isolated from kimchi

Journal of Applied Microbiology, 2021
This study aimed to screen the γ‐aminobutyric acid (GABA)‐producing lactic acid bacteria (LAB) from kimchi, and investigate the glutamate decarboxylase (GAD) activity of the highest GABA‐producing strain.
Wenli Liu, Huamin Li, Long Liu, K. Ko, Incheol Kim   +4 more
semanticscholar   +1 more source

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
openaire   +2 more sources

Glutamate decarboxylase and its isoforms

Medical academic journal
The review summarizes current data on the properties, localization and physiological role of GABA synthesizing enzyme, glutamic acid decarboxylase, in mammalian tissues.
Valeriia A. Razenkova, D. Korzhevskii
semanticscholar   +1 more source

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
openaire   +1 more source

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
openaire   +2 more sources

Stereochemistry of reactions catalyzed by glutamate decarboxylase

Biochemistry, 1978
When the decarboxylation of L-glutamic acid by the glutamate decarboxylase from Escherichia coli is carried out in D2O, the product gamma-aminobutyric acid contains a single deuterium atom. The stereochemistry of this material was established by conversion to levorotatory methyl 4-phthalimido [4(-2)H] butyrate.
H, Yamada, M H, O'Leary
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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.
openaire   +2 more sources

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
openaire   +2 more sources