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

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Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.). / Creissen, G.; Edwards, E. A.; Enard, C. et al.
In: The Plant Journal, Vol. 2, No. 1, 1992, p. 129-131.

Research output: Contribution to Journal/Magazine › Journal article

Harvard

Creissen, G, Edwards, EA, Enard, C, Wellburn, AR & Mullineaux, P 1992, 'Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.).', The Plant Journal, vol. 2, no. 1, pp. 129-131. https://doi.org/10.1111/j.1365-313X.1992.00129.x

APA

Creissen, G., Edwards, E. A., Enard, C., Wellburn, A. R., & Mullineaux, P. (1992). Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.). The Plant Journal, 2(1), 129-131. https://doi.org/10.1111/j.1365-313X.1992.00129.x

Vancouver

Creissen G, Edwards EA, Enard C, Wellburn AR, Mullineaux P. Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.). The Plant Journal. 1992;2(1):129-131. doi: 10.1111/j.1365-313X.1992.00129.x

Author

Creissen, G. ; Edwards, E. A. ; Enard, C. et al. / Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.). In: The Plant Journal. 1992 ; Vol. 2, No. 1. pp. 129-131.

Bibtex

@article{2a2b1404551243e9af60c1d0a46b1d52,
title = "Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.).",
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.",
author = "G. Creissen and Edwards, {E. A.} and C. Enard and Wellburn, {A. R.} and P. Mullineaux",
year = "1992",
doi = "10.1111/j.1365-313X.1992.00129.x",
language = "English",
volume = "2",
pages = "129--131",
journal = "The Plant Journal",
publisher = "Blackwell Publishing Ltd",
number = "1",

}

RIS

TY - JOUR

T1 - Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.).

AU - Creissen, G.

AU - Edwards, E. A.

AU - Enard, C.

AU - Wellburn, A. R.

AU - Mullineaux, P.

PY - 1992

Y1 - 1992

N2 - 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.

AB - 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.

U2 - 10.1111/j.1365-313X.1992.00129.x

DO - 10.1111/j.1365-313X.1992.00129.x

M3 - Journal article

VL - 2

SP - 129

EP - 131

JO - The Plant Journal

JF - The Plant Journal

IS - 1

ER -