S- aminoethyl- l -cysteine transaminase from bovine brain: purification to homogeneity and assay of activity in different regions of the brain.

@article{Pensa1989SAL,
  title={S- aminoethyl- l -cysteine transaminase from bovine brain: purification to homogeneity and assay of activity in different regions of the brain.},
  author={B Pensa and Marco Achilli and Mario Fontana and Anna Maria Caccuri and Doriano Cavallini},
  journal={Neurochemistry international},
  year={1989},
  volume={15 3},
  pages={285-91}
}
A transminase acting on cystathionine, S-aminoethylcysteine and glutamine has been purified to homogeneity from bovine brain by ammonium sulfate precipitation. DE-52 chromatography, octyl-Sepharose chromatography, hydroxylapatite chromatography and gel filtration. The enzyme was purified 4700 times over the bovine brain homogenate and the overall recovery of the enzyme activity was about 18%. As demonstrated by polyacrylamide gel electrophoresis under native or denaturing conditions, the enzyme… CONTINUE READING