A unique proenkephalin-converting enzyme purified from bovine adrenal chromaffin granules

Kensaku Mizuno, Atsuro Miyata, Kenji Kangawa, Hisayuki Matsuo

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)

Abstract

A unique proenkephalin converting enzyme specifically generating enkephalin was partially purified from lysates of adrenal chromaffin granules. The enzyme, whose molecular weight is estimated as ca. 220,000, is thiol-dependent protease, with optimal pH at around 5.5. The enzyme converts proenkephalin to enkephalins by cleaving specifically at the sites of consecutive basic amino acid residues. The enzyme also converts BAM-12P, an adrenal "big" Met-enkephalin, to Met-enkephalin in a similar manner. During the enzyme reaction, formation of [Arg6]-Met-enkephalin was not observed. Additionally, [Arg6]-enkephalins were not converted to enkephalins by the enzyme. Consequently, the enzyme was proved to be a unique converting enzyme distinct from either trypsin-like or carboxypeptidase B-like proteases.

Original languageEnglish
Pages (from-to)1235-1242
Number of pages8
JournalBiochemical and biophysical research communications
Volume108
Issue number3
DOIs
Publication statusPublished - 1982 Oct 15
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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