Purification and characterization of a neuropeptide-degrading aminopeptidase from human brain.

@article{McDermott1985PurificationAC,
  title={Purification and characterization of a neuropeptide-degrading aminopeptidase from human brain.},
  author={Jessica McDermott and David Mantle and B L Lauffart and Alexa M J Kidd},
  journal={Journal of neurochemistry},
  year={1985},
  volume={45 3},
  pages={752-9}
}
The major aminopeptidase from human post-mortem brain (occipital cortex) was purified to homogeneity (as judged by polyacrylamide gel electrophoresis) by anion-exchange chromatography (two steps) and gel filtration (two steps). The molecular weight of the enzyme was estimated as 105,000 from gel filtration. Maximum activity was obtained in the presence of 0.5 mM Ca2+ and 1 mM 2-mercaptoethanol at pH 7.3. Enzyme activity was lost on freezing and thawing or on lyophilization. The enzyme was… CONTINUE READING

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