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- W1995896282 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 invitro 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." @default.
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- W1995896282 date "1990-03-01" @default.
- W1995896282 modified "2023-10-14" @default.
- W1995896282 title "Cleavage of recombinant enkephalin precursor by endoproteolytic activity in bovine chromaffin granules" @default.
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- W1995896282 doi "https://doi.org/10.1016/0006-291x(90)92085-e" @default.
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