Results 81 to 90 of about 1,586 (109)
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Biochemical Pharmacology, 2006
The use of the antiepileptic drug, 4-aminobutyrate transaminase (GABA-T) inhibitor vigabatrin (VIGA), has been recently cautioned because it is associated to irreversible field defects from damage of the retina. Since novel GABA-T inhibitors might prove useful in epilepsy or other CNS pathologies as VIGA substitutes, the aim of the present ...
Maria Frosini +2 more
exaly +6 more sources
The use of the antiepileptic drug, 4-aminobutyrate transaminase (GABA-T) inhibitor vigabatrin (VIGA), has been recently cautioned because it is associated to irreversible field defects from damage of the retina. Since novel GABA-T inhibitors might prove useful in epilepsy or other CNS pathologies as VIGA substitutes, the aim of the present ...
Maria Frosini +2 more
exaly +6 more sources
Two Forms of 4-Aminobutyrate Transaminase in Guinea Pig Brain
Enzyme, 20174-Aminobutyrate transaminase (GABA-T, 4-aminobutyrate α-oxoglutarate aminotransferase, EC 2.6.1.19) is an enzyme that inactivates the inhibitory neurotransmitter, GABA, but its pharmacological function is uncertain. Two forms of guinea pig brain GABA-T were isolated by DEAE-cellulose chromatography and designated as GABA-T-I and II, corresponding to an
P P, Ho, A L, Young, P C, Walters
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Acta Histochemica, 1986
A pharmaco-histochemical method for demonstrating the enzyme 4-aminobutyrate: 2-oxoglutarate transaminase was applied to the sections of the rat supraoptic nucleus region. The reactions of GABAergic interneurons and their relationship to neurosecretory neurons were studied.
K, Iijima, N, Kojima
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A pharmaco-histochemical method for demonstrating the enzyme 4-aminobutyrate: 2-oxoglutarate transaminase was applied to the sections of the rat supraoptic nucleus region. The reactions of GABAergic interneurons and their relationship to neurosecretory neurons were studied.
K, Iijima, N, Kojima
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Journal of Neurochemistry, 1974
Abstract— The effects of divalent metal ions, sulfhydryl reagents, carbonyl trapping reagents, substrate analogs, and organic solvents on purified mouse brain 4‐aminobutyrate‐2‐ketoglutarate transaminase (EC 2.6.1.19) and the subunit structure of this enzyme were studied.
A, Schousboe, J Y, Wu, E, Roberts
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Abstract— The effects of divalent metal ions, sulfhydryl reagents, carbonyl trapping reagents, substrate analogs, and organic solvents on purified mouse brain 4‐aminobutyrate‐2‐ketoglutarate transaminase (EC 2.6.1.19) and the subunit structure of this enzyme were studied.
A, Schousboe, J Y, Wu, E, Roberts
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Journal of Neurochemistry, 1977
Abstract— The activity of 4‐aminobutyric‐2‐oxoglutaric acid transaminase (GABA transaminase) and succinic semialdehyde dehydrogenase was determined in total rat brain homogenate. GABA transaminase activity was measured using a coupled enzyme method which utilizes endogenous succinic semialdehyde dehydrogenase to convert the formed succinic semialdehyde
T, De Boer, J, Bruinvels
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Abstract— The activity of 4‐aminobutyric‐2‐oxoglutaric acid transaminase (GABA transaminase) and succinic semialdehyde dehydrogenase was determined in total rat brain homogenate. GABA transaminase activity was measured using a coupled enzyme method which utilizes endogenous succinic semialdehyde dehydrogenase to convert the formed succinic semialdehyde
T, De Boer, J, Bruinvels
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Biochimica et Biophysica Acta (BBA) - Enzymology, 1978
4-Aminobutyrate:2-oxoglutarate (4-aminobutyrate:2-oxoglutarate amino-transferase, EC 2.6.1.19) from human brain has been purified 2500-fold with respect to the initial homogenate. The enzyme, which appears to be pure by polyacrylamide gel electrophoresis, N-terminal analysis and immunodiffusion, was compared to rat brain 4-aminobutyrate transaminase ...
M, Maitre +3 more
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4-Aminobutyrate:2-oxoglutarate (4-aminobutyrate:2-oxoglutarate amino-transferase, EC 2.6.1.19) from human brain has been purified 2500-fold with respect to the initial homogenate. The enzyme, which appears to be pure by polyacrylamide gel electrophoresis, N-terminal analysis and immunodiffusion, was compared to rat brain 4-aminobutyrate transaminase ...
M, Maitre +3 more
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Biochemical and Biophysical Research Communications, 1982
Abstract γ-Aminobutyric acid-α-ketoglutarate aminotransferase from rat and mouse brain was irreversibly inhibited by 5-fluoro-4-oxo-pentanoic acid, an analogue of succinic semi-aldehyde. The inhibition was concentration and temperature-dependent, and was initiated solely with the pyridoxamine form of the enzyme.
B, Lippert, B W, Metcalf, R J, Resvick
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Abstract γ-Aminobutyric acid-α-ketoglutarate aminotransferase from rat and mouse brain was irreversibly inhibited by 5-fluoro-4-oxo-pentanoic acid, an analogue of succinic semi-aldehyde. The inhibition was concentration and temperature-dependent, and was initiated solely with the pyridoxamine form of the enzyme.
B, Lippert, B W, Metcalf, R J, Resvick
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Experientia, 1976
The two forms isolated exhibit some differences concerning their physicochemical and functional properties. They are identical with the previously purified molecular fomrs, GABAT I and GABAT II, separated by DEAE cellulose chromatography.
M. Tardy +3 more
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The two forms isolated exhibit some differences concerning their physicochemical and functional properties. They are identical with the previously purified molecular fomrs, GABAT I and GABAT II, separated by DEAE cellulose chromatography.
M. Tardy +3 more
openaire +1 more source