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

✍ Scribed by Gary Creissen; E. Anne Edwards; Corine Enard; Alan Wellburn; Phil Mullineaux

Publisher
John Wiley and Sons
Year
1992
Tongue
English
Weight
312 KB
Volume
2
Category
Article
ISSN
0960-7412

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✦ Synopsis

Summary

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.

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