Purification and characterization of an enkephalin aminopeptidase from rat brain membranes.

@article{Hui1983PurificationAC,
  title={Purification and characterization of an enkephalin aminopeptidase from rat brain membranes.},
  author={Kin Hui and Y. John Wang and Abel Lajtha},
  journal={Biochemistry},
  year={1983},
  volume={22 5},
  pages={1062-7}
}
A membrane-bound aminopeptidase was purified from rat brain, and its activity was assayed by high-pressure liquid chromatography with Met-enkephalin as the substrate. The enzyme was extracted with 1% Triton X-100 and purified by chromatography, successively on DEAE-Sepharose CL-6B, Bio-Gel HTP, and Sephadex G-200 columns. The overall purification was about 1200-fold, with 25% yield. The purified enzyme showed one band on disc gel electrophoresis and two bands on sodium dodecyl sulfate… CONTINUE READING