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Dynorphin converting enzyme with unusual specificity from rat brain.

L Devi·A Goldstein
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Abstract

A rat brain membrane extract was shown to convert synthetic dynorphin B-29 ("leumorphin") to dynorphin B [dynorphin B-29-(1-13), "rimorphin"]. This represents a "single arginine cleavage" at Thr-Arg at positions 13 and 14 of the substrate. The product was identified by immunoprecipitation with a highly specific dynorphin B antiserum and by coelution with radiolabeled dynorphin B on reversed-phase high-performance liquid chromatography. The converting activity exhibits a pH optimum of 8. It is inhibited by a thiol protease inhibitor but not by inhibitors of cathepsin B or of serine proteases. It is inhibited by dynorphin A but not by various dynorphin A fragments. These results suggest that the converting activity is due to a novel thiol protease distinct from any known protease believed to function in the processing of biologically active peptides.

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AnimalsBrainCysteine EndopeptidasesDynorphinsEndopeptidasesEndorphinsEnkephalinsHydrogen-Ion ConcentrationKineticsMalePeptide FragmentsProtease InhibitorsProtein PrecursorsRatsSubstrate SpecificityJournal ArticleResearch Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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L Devi, A Goldstein. 1984. Dynorphin converting enzyme with unusual specificity from rat brain.. https://doi.org/10.1073/pnas.81.6.1892

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