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Conversion of Leumorphin (Dynorphin B‐29) to Dynorphin B and Dynorphin B‐14 by Thiol Protease Activity
Author(s) -
Devi Lakshmi,
Goldstein Avram
Publication year - 1986
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1986.tb02843.x
Subject(s) - dynorphin , dynorphin a , chemistry , protease , arginine , biochemistry , opioid peptide , amino acid , enzyme , opioid , receptor
Dynorphin B (rimorphin) is formed from leumorphin (dynorphin B‐29) by the action of a thiol protease from rat brain membranes, in a single step. This represents a “single‐arginine cleavage” between threonine‐13 and arginine‐14 of the substrate. We have observed that in addition to dynorphin B, dynorphin B‐14 is formed from dynorphin B‐29. Among the various protease inhibitors tested, none except p ‐chloromercuriben‐zensulfonic acid inhibited the formation of the two products. Both temperature and pH had similar effects on the formation of dynorphin B‐14 and dynorphin B. The inhibitory potencies of adrenocorticotropic hormone, peptide E, and dynorphin A were virtually identical for the formation of the two products. These results suggest that the same enzyme may be responsible for the formation of dynorphin B‐14 and dynorphin B.