Abstract
SDS-polyacrylamide electrophoresis of a partially purified trypsin-like enzyme obtained from bovine adrenal chromaffin granules revealed that considerable purification of the enzymatic activity from other soluble granule proteins was achieved by affinity chromatography over soybean trypsin inhibitor affinity columns. This partially purified enzyme preparation was able to hydrolyze Peptide F to produce low molecular weight enkephalin-immunoreactive peptides. The pH optimum of enkephalin-IR generating activity using endogenous substrate(s) was determined to 8.0.
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