Results 131 to 140 of about 2,830 (156)
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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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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
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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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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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Archives of Biochemistry and Biophysics, 1979
Abstract Some kinetic properties of two new species of transaminase found in extracts of a β-lysine-utilizing Pseudomonas are reported. Transaminase A catalyzes transamination between 6- N -acetyl- l -β-lysine (3-amino-6-acetamidohexanoate) and α-ketoglutarate to form 3-keto-6-acetamidohexanoate and glutamate.
G, Bozler +4 more
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Abstract Some kinetic properties of two new species of transaminase found in extracts of a β-lysine-utilizing Pseudomonas are reported. Transaminase A catalyzes transamination between 6- N -acetyl- l -β-lysine (3-amino-6-acetamidohexanoate) and α-ketoglutarate to form 3-keto-6-acetamidohexanoate and glutamate.
G, Bozler +4 more
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[Inhibition of 4-aminobutyrate transaminase by ethanolamine-O-sulfate].
Biokhimiia (Moscow, Russia), 1977The analysis of the interaction of ethanolamine-O-sulphate with 4-aminobutyrate transaminase revealed that the inhibitory effect is exerted upon the substrate subsite of the active site of the enzyme in aldimine form. The inhibition in irreversible. The inactivation rate versus pH-curve was shown to have a sigmoid character with inclination point at ...
V Iu, Vasil'ev, E B, Krylova
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Biokhimiia (Moscow, Russia), 1977
The study of interaction of 4-aminobutyrate transaminase with 5'- 6'-methyl derivates of PLP demonstrated that only the former was capable of forming a catalytically active holoenzyme possessing 0.37 activity of the native holoenzyme and a low affinity substrates.
V Iu, Vasil'ev +2 more
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The study of interaction of 4-aminobutyrate transaminase with 5'- 6'-methyl derivates of PLP demonstrated that only the former was capable of forming a catalytically active holoenzyme possessing 0.37 activity of the native holoenzyme and a low affinity substrates.
V Iu, Vasil'ev +2 more
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About species specificity of brain 4‐aminobutyrate‐2‐ketoglutarate transaminase (GABAT)
Journal of Neurochemistry, 1976M, Tardy +3 more
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