An enkephalin-generating enzyme in bovine adrenal medulla
Lindberg, I.; Yang, H.Y.; Costa, E.
Biochemical and Biophysical Research Communications 106(1): 186-193
1982
ISSN/ISBN: 0006-291X PMID: 7049167 Document Number: 190181
A trypsin-like enzyme was partially purified from bovine adrenal chromaffin granules through the use of affinity chromatography. This enzyme preparation was able to generate met5-enkephalin from endogenous substrate(s). Met5-enkephalin production was not inhibited by sulfhydryl reagents such as p-chloromercuriphenyl sulfonate nor stimulated by dithiothreitol, suggesting that this enzyme is not a lysosomal enzyme such as cathepsin B. Enzymatic activity was strongly inhibited by several trypsin inhibitors including soybean trypsin inhibitor, aprotinin and DFP. Apparently this adrenal enkephalin-generating enzyme is a serine protease.