Purification and characterization of a novel neurotensin-degrading peptidase from rat brain synaptic membranes.

@article{Checler1986PurificationAC,
  title={Purification and characterization of a novel neurotensin-degrading peptidase from rat brain synaptic membranes.},
  author={Fr{\'e}d{\'e}ric Checler and J. P. Vincent and Patrick Kitabgi},
  journal={The Journal of biological chemistry},
  year={1986},
  volume={261 24},
  pages={11274-81}
}
A peptidase that cleaved neurotensin at the Pro10-Tyr11 peptide bond, leading to the formation of neurotensin-(1-10) and neurotensin-(11-13), was purified nearly to homogeneity from rat brain synaptic membranes. The enzyme appeared to be monomeric with a molecular weight of about 70,000-75,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and high pressure liquid chromatography filtration. Isoelectrofocusing indicated a pI of 5.9-6. The purified peptidase could be… CONTINUE READING
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