Purification and characterization of a peptide C-terminal α-amidating enzyme from porcine atrium

Masayasu Kojima, Kensaku Mizuno, Kenji Kangawa, Hisayuki Matsuo

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13 Citations (Scopus)

Abstract

In many peptide hormones and neuropeptides, the carboxy-terminal α-amide structure is essential in eliciting biological activity. Here we report the purification and characterization of an α-amidating enzyme from porcine atrium, in which a high concentration of α-amidating activity was detected. The enzyme was purified to homogeneity from the membrane fraction of porcine atria by five steps of chromatography, including an affinity chromatography using a Sepharose column coupled with a substrate, Tyr-Phe-Gly. The purified enzyme was found to be composed of a single polypeptide chain with an apparent molecular weight of 92,000. This enzyme converted several synthetic peptides with C-terminal glycine to the corresponding des-glycine peptide α-amides.

Original languageEnglish
Pages (from-to)440-443
Number of pages4
JournalJournal of biochemistry
Volume105
Issue number3
DOIs
Publication statusPublished - 1989 Mar
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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