Function of neutral endopeptidase on the cell membrane of human neutrophils.

@article{Painter1988FunctionON,
  title={Function of neutral endopeptidase on the cell membrane of human neutrophils.},
  author={Richard G. Painter and Richard L. Dukes and J Sullivan and RobertB. Carter and Ervin G. Erd{\"o}s and Adam R. Johnson},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 19},
  pages={
          9456-61
        }
}
Intact human neutrophils hydrolyzed N-formyl-Met-Leu-[3H]Phe (fMLP) and released Leu-[3H]Phe, cleaving 45-50% of the peptide within 20 min at 37 degrees C. The dipeptide after its release was then hydrolyzed to free amino acids by a dipeptidase (EC 3.4.13.11). This activity, present in plasma membrane-enriched fractions of neutrophil lysates, was also inhibited over 90% by phosphoramidon, an inhibitor of neutral endopeptidase (NEP, EC 3.4.24.11). Dithiothreitol and EDTA inhibited the activity… CONTINUE READING

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