An aminopeptidase solubilized and isolated from rat brain membranes selectively splits the Tyr1-Gly2 peptide bond of Met-enkephalin. βh-Endorphin, which is apparently resistant to the aminopeptidase, inhibited the action of this peptidase on Met-enkephalin degradation competitively; the Ki value was 11.5 μM. Arg0-βh-endorphin was found to be 10 times more potent than βh-endorphin. From further structure-activity data it is concluded that the N-terminal amino group and some residues within region 18-31 of the β-endorphin structure are cooperatively involved in binding to the active site of the aminopeptidase.
|Number of pages||6|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - Apr 29 1982|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology