Cleavage of recombinant enkephalin precursor by endoproteolytic activity in bovine chromaffin granules.

Abstract:

:To identify endoproteolytic activity that processes the enkephalin precursor, a novel approach was undertaken for the production of model substrate in the form of recombinant 35S-(Met)-preproenkephalin (35S-(Met)-PPE), generated by in vitro transcription and translation of the rat PPE cDNA. Endoproteolytic activity in bovine chromaffin granules cleaved 35S-(Met)-PPE with a pH optimum of 4.5 and generated multiple products containing the NH2-terminal segment of the precursor. Processing of 35S-(Met)-PPE, as well as endogenous enkephalin intermediates, was inhibited by pepstatin A and stimulated by DTT. These results suggest that aspartyl and thiol proteolytic activity(ies) are involved in cleaving the enkephalin precursor.

authors

Hook VY,Hegerle D,Affolter HU

doi

10.1016/0006-291x(90)92085-e

subject

Has Abstract

pub_date

1990-03-16 00:00:00

pages

722-30

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(90)92085-E

journal_volume

167

pub_type

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