Purification, characterization and inhibition of D-3-aminoisobutyrate aminotransferase from the rat liver.

@article{Tamaki1990PurificationCA,
  title={Purification, characterization and inhibition of D-3-aminoisobutyrate aminotransferase from the rat liver.},
  author={N. Tamaki and M. Kaneko and C. Mizota and M. Kikugawa and S. Fujimoto},
  journal={European journal of biochemistry},
  year={1990},
  volume={189 1},
  pages={
          39-45
        }
}
D-3-Aminoisobutyrate-pyruvate aminotransferase was purified 2000-fold from rat liver extract using heat treatment, ammonium sulfate fractionation, carboxylmethyl-Sepharose CL-6B, DEAE-Sepharose CL-6B, hydroxyapatite, Sephacryl S-200 and electrofocusing chromatographies. The purified enzyme was shown to be homogeneous by gel electrophoresis both in the presence and absence of SDS. Its molecular mass, determined by gel filtration, was 220 kDa and the subunit molecular mass was 52 kDa. The enzyme… Expand
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References

SHOWING 1-10 OF 39 REFERENCES
4-Aminobutyrate aminotransferase. The presence of nonequivalent binding sites.
  • 57
...
1
2
3
4
...