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Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.).

Research output: Contribution to journalJournal article

Published
  • G. Creissen
  • E. A. Edwards
  • C. Enard
  • A. R. Wellburn
  • P. Mullineaux
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<mark>Journal publication date</mark>1992
<mark>Journal</mark>The Plant Journal
Issue number1
Volume2
Number of pages3
Pages (from-to)129-131
Publication StatusPublished
<mark>Original language</mark>English

Abstract

A cDNA for pea glutathione reductase has been cloned and sequenced. The derived amino acid sequence of 562 residues shows a high degree of homology to the previously published GR sequences from human erythrocytes and from two prokaryotes: Escherichia coli and Pseudomonas aeruginosa. The pea enzyme differs from other GRs in having an M-terminal leader sequence of about 60–70 residues which may be a chloroplast transit peptide and a 20 amino acid C-terminal extension of unknown function.