Abstract: The kinetics of the reactions of nine opioid peptides with the neutral endopeptidase (“enkephalinase”) activities of human kidney, rat kidney, and rat brain have been determined. These opioid peptides can be divided into two classes, those that are good inhibitors of Leu5‐enkephalin hydrolysis (K1 < 75 μM) and good substrates for the enzyme, and those that are poor inhibitors (K1 > 500 μM) and are not substrates for the enzyme. The former group includes Leu5‐enkephalin, Met5‐enkephalin, Met5‐enkephalin‐Arg6‐Phe7, β‐lipotropin6169, and γ‐endorphin, while the nonreactive opioid peptides include α‐neo‐endorphin, β‐neo‐endorphin, dynorphin1–13, and β‐endorphin. These results suggest that those peptides containing the Met5‐enkephalin sequence are more reactive than those containing the Leu5‐enkephalin sequence. The lack of specificity of this neutral endopeptidase indicates that it may function in the degradation of a variety of biologically active peptides.
|Number of pages||7|
|Journal||Journal of Neurochemistry|
|State||Published - Aug 1984|
- Neutral endopeptidase
- Opioid peptides
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience