Paired basic residues, particularly Lys-Arg, are known as a typical site for proteolytic processing of prohormones. In this study, we confirmed the presence of a novel protease exhibiting substrate specificity toward Lys-Arg sequence. It was partially purified from the soluble fraction of bovine adrenomedullary chromaffin granules by using an affinity chromatography on soybean trypsin inhibitor-Sepharose. The enzyme, with optimal pH around 7.5-9.5, is classified into a serine-protease family by its inhibition spectrum. The enzyme specifically cleaves in between the Lys-Arg bonds of the peptides related to proenkephalins, but the sequences of Arg-Arg, Arg-Lys and a single basic residue (Arg or Lys) in the substrates are not affected by the enzyme. The unique substrate specificity of the enzyme suggests that it is distinct from pancreatic trypsin and may be physiologically involved in proenkephalin processing.
|Number of pages||8|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - 1985 Apr 30|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology