Abstract
A novel protease exhibiting substrate specificity toward paired basic residues has been partially purified from the soluble fraction of bovine adrenal chromaffin granules by utilizing an affinity chromatography on STI-Sepharose. The enzyme, with optimal pH around 7.5-9.5, is classified into a serine-protease by its inhibitor spectrum. The enzyme specifically cleaved the Lys-Arg bonds of two synthetic peptides containing the subsequence of proenkephalin A, but endogenous opioid peptides containing a single basic residue in the molecule ((Met)enk-Arg-Phe, (Met)enk-Arg-Gly-Leu) were not affected by the enzyme. The unique substrate specificity of the enzyme, which is well in accord with the processing pattern of proenkephalin A in adrenal medulla, indicates that the enzyme may be physiologically involved in proenkephalin processing.
Original language | English |
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Pages (from-to) | 489-492 |
Number of pages | 4 |
Journal | Neuropeptides |
Volume | 5 |
Issue number | 4-6 |
DOIs | |
Publication status | Published - 1985 Jan 1 |
Externally published | Yes |
ASJC Scopus subject areas
- Endocrinology
- Neurology
- Endocrine and Autonomic Systems
- Cellular and Molecular Neuroscience