Results 91 to 100 of about 1,586 (109)
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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
openaire +2 more sources
[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
openaire +1 more source
About species specificity of brain 4‐aminobutyrate‐2‐ketoglutarate transaminase (GABAT)
Journal of Neurochemistry, 1976M, Tardy +3 more
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