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

doi:10.1016/S0014-5793(98)00311-1

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 journal › Article › peer-review

Abstract

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 language	English
Pages (from-to)	62-66
Number of pages	5
Journal	FEBS Letters
Volume	426
Issue number	1
DOIs	https://doi.org/10.1016/S0014-5793(98)00311-1
Publication status	Published - Apr 10 1998

Keywords

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

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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10.1016/S0014-5793(98)00311-1

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Maize polyamine oxidase : Primary structure from protein and cDNA sequencing. / Tavladoraki, Paraskevi; Schininà, M. Eugenia; Cecconi, Francesco; Di Agostino, Silvia; Manera, Francesco; Rea, Giuseppina; Mariottini, Paolo; Federico, Rodolfo; Angelini, Riccardo.

In: FEBS Letters, Vol. 426, No. 1, 10.04.1998, p. 62-66.

Research output: Contribution to journal › Article › peer-review

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abstract = "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.",

keywords = "Flavin oxidase, Hydrogen peroxide, Polyamine oxidase, Primary structure, Zea mays L.",

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T2 - Primary structure from protein and cDNA sequencing

AU - Tavladoraki, Paraskevi

AU - Schininà, M. Eugenia

AU - Cecconi, Francesco

AU - Di Agostino, Silvia

AU - Manera, Francesco

AU - Rea, Giuseppina

AU - Mariottini, Paolo

AU - Federico, Rodolfo

AU - Angelini, Riccardo

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AB - 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.

KW - Flavin oxidase

KW - Hydrogen peroxide

KW - Polyamine oxidase

KW - Primary structure

KW - Zea mays L.

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Maize polyamine oxidase: Primary structure from protein and cDNA sequencing

Abstract

Keywords

ASJC Scopus subject areas

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