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Maize polyamine oxidase: primary structure from protein and cDNA sequencing

Academic Article
Publication Date:
1998
abstract:
The first complete amino acid sequence of a flavincontaining 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.
Iris type:
01.01 Articolo in rivista
Keywords:
Flavin oxidase; Hydrogen peroxide; Polyamine oxidase
List of contributors:
Rea, Giuseppina
Authors of the University:
REA GIUSEPPINA
Handle:
https://iris.cnr.it/handle/20.500.14243/223860
Published in:
FEBS LETTERS
Journal
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