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- W2021599018 abstract "Beef brain cytoplasmic aspartate aminotransferase (l-aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1) was purified 380-fold. The existence of multiple forms (α, β, γ) of the enzyme was shown by chromatography on Sephadex CM-50 at pH 5.4 and by electrophoresis at pH 9.0 on plyacrylamide gel. Analytical ultracentrifugation yielded a sedimentation coefficient of 5.62 S and a mol. wt of 90 000 ± 6000 for the brain aspartate aminotransferase. A Stokes radius of 39.5 Å and a mol. wt of 103 000 were determined for the enzyme by gel filtration on Sephadex G-200. Apparent Km values of 2 mM for l-aspartate and 0.17 mM for α-ketoglutarate were obtained with the brain aspartate aminotransferase. The enzyme was inhibited significantly by 1–3 mM α-ketoglutarate at pH 6.0. No inhibition of brain aspartate aminotransferase activity was noted with γ-aminobutyric acid. Most of these properties of the beef brain enzyme are the same as those obtained with beef heart cytoplasmic aspartate aminotransferase." @default.
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- W2021599018 date "1973-05-01" @default.
- W2021599018 modified "2023-10-15" @default.
- W2021599018 title "Beef brain cytoplasmic aspartate aminotransferase. Purification, kinetics, and physical properties" @default.
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- W2021599018 doi "https://doi.org/10.1016/0005-2744(73)90320-3" @default.
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