Proenkephalin processing enzyme with specificity toward paired basic residues purified from bovine adrenal chromaffin granules

Kensaku Mizuno, Hisayuki Matsuo

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

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 languageEnglish
Pages (from-to)489-492
Number of pages4
JournalNeuropeptides
Volume5
Issue number4-6
DOIs
Publication statusPublished - 1985 Jan 1
Externally publishedYes

ASJC Scopus subject areas

  • Endocrinology
  • Neurology
  • Endocrine and Autonomic Systems
  • Cellular and Molecular Neuroscience

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