Cleavage of recombinant enkephalin precursor by endoproteolytic activity in bovine chromaffin granules.
作者信息
Hook V Y, Hegerle D, Affolter H U
机构信息
Department of Biochemistry, Uniformed Services University of the Health Sciences, Bethesda, MD 20814.
出版信息
Biochem Biophys Res Commun. 1990 Mar 16;167(2):722-30. doi: 10.1016/0006-291x(90)92085-e.
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.
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