Unknown

Dataset Information

0

The metabolism of neuropeptides. Both phosphoramidon-sensitive and captopril-sensitive metallopeptidases are present in the electric organ of Torpedo marmorata.


ABSTRACT: A membrane fraction from the electric organ of Torpedo marmorata hydrolyses the Gly3-Phe4 bond of [D-Ala2, Leu5]enkephalin as well as the Gly-His bond of benzoyl-Gly-His-Leu. The hydrolysis of benzoyl-Gly-His-Leu is completely inhibitable by Captopril (I50 = 19nM), consistent with peptidyl dipeptidase activity, but enkephalin hydrolysis is inhibited to a maximum of only 70%. The residual activity hydrolysing enkephalin is inhibited by phosphoramidon (I50 = 15nM) and therefore resembles endopeptidase-24.11, a mammalian plasma-membrane enzyme implicated in the metabolism of neuropeptides. Both enkephalin-hydrolysing activities in Torpedo electric organ are inhibited by 1,10-phenanthroline, like their mammalian counterparts. The peptidases may function in the hydrolysis of endogenous peptides or in neurotransmitter exocytosis in the electric organ.

SUBMITTER: Turner AJ 

PROVIDER: S-EPMC1144167 | biostudies-other | 1984 Aug

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1164010 | biostudies-other
2011-06-23 | PRD000388 | Pride
| S-EPMC1164206 | biostudies-other
| S-EPMC1151468 | biostudies-other
| S-EPMC1161053 | biostudies-other
| S-EPMC1165028 | biostudies-other
| S-EPMC3412124 | biostudies-literature
| S-EPMC1132579 | biostudies-other
| S-EPMC1137719 | biostudies-literature
| S-EPMC1218370 | biostudies-other