Purification and studies on some properties of the 4-aminobutyrate : 2-oxoglutarate transaminase from rat brain.

@article{Maitre1975PurificationAS,
  title={Purification and studies on some properties of the 4-aminobutyrate : 2-oxoglutarate transaminase from rat brain.},
  author={Michel Maitre and Leigh Ciesielski and Christopher D. Cash and Paul Mandel},
  journal={European journal of biochemistry},
  year={1975},
  volume={52 1},
  pages={157-69}
}
Using various chromatographic procedures, 4-aminobutyrate : 2-oxoglutarate transaminase from rat brain has been purified 2400 times with respect to the initial brain homogenate. The purified protein, which has a specific activity of 10 mumol times min -1, x mg-1 gave a single band by acrylamide gel electrophoresis and isoelectric focusing. It has a molecular weight of 105000 +/- 5000 and an isoelectric point of 6.8. In the presence of 0.1% sodium dodecylsulphate, a single protein band is seen… CONTINUE READING

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