Neurotensin-metabolizing peptidases in rat fundus plasma membranes.

@article{Checler1987NeurotensinmetabolizingPI,
  title={Neurotensin-metabolizing peptidases in rat fundus plasma membranes.},
  author={Fr{\'e}d{\'e}ric Checler and H{\'e}l{\`e}ne Barelli and Chiu-yin Kwan and Patrick Kitabgi and J. P. Vincent},
  journal={Journal of neurochemistry},
  year={1987},
  volume={49 2},
  pages={507-12}
}
The mechanisms by which neurotensin (NT) was inactivated by rat fundus plasma membranes were characterized. Primary inactivating cleavages occurred at the Arg8-Arg9, Pro10-Tyr11, and Ile12-Leu13 peptidyl bonds. Hydrolysis at the Arg8-Arg9 bond was fully abolished by the use of N-[1(R,S)-carboxy-2-phenylethyl]-alanyl-alanyl-phenylalanine-p- aminobenzoate, a result indicating the involvement at this site of a recently purified soluble metallopeptidase. Hydrolysis of the Pro10-Tyr11 bond was… CONTINUE READING

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