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

Creissen, G. and Edwards, E. A. and Enard, C. and Wellburn, A. R. and Mullineaux, P. (1992) Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.). The Plant Journal, 2 (1). pp. 129-131.

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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.

Item Type: Article
Journal or Publication Title: The Plant Journal
Subjects: G Geography. Anthropology. Recreation > GE Environmental Sciences
Departments: Faculty of Science and Technology > Lancaster Environment Centre
ID Code: 22749
Deposited By: ep_ss_importer
Deposited On: 13 Jan 2009 10:32
Refereed?: No
Published?: Published
Last Modified: 26 Jul 2012 16:05
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/22749

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