Maize polyamine oxidase: Primary structure from protein and cDNA sequencing

Paraskevi Tavladoraki, M. Eugenia Schininà, Francesco Cecconi, Silvia Di Agostino, Francesco Manera, Giuseppina Rea, Paolo Mariottini, Rodolfo Federico, Riccardo Angelini

Research output: Contribution to journalArticlepeer-review


The first complete amino acid sequence of a flavin-containing polyamine oxidase was solved by a combined approach of nucleotide and peptide sequence analysis. A cDNA of 1737 bp, isolated from maize seedlings by reverse transcription-polymerase chain reaction and rapid amplification of cDNA ends strategies, was cloned and its sequence determined. This cDNA contains information for a polypeptide chain of 500 amino acids. Its amino-terminal sequence shows the typical features of secretion signal peptides. The primary structure of the mature protein was independently confirmed by extensive amino acid sequencing. Structural relationships with flavin-containing monoamine oxidases are also discussed.

Original languageEnglish
Pages (from-to)62-66
Number of pages5
JournalFEBS Letters
Issue number1
Publication statusPublished - Apr 10 1998


  • Flavin oxidase
  • Hydrogen peroxide
  • Polyamine oxidase
  • Primary structure
  • Zea mays L.

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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