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Edwards EA, Rawsthorne S, Mullineaux PM. Subcellular distribution of multiple forms of glutathione reductase in leaves of pea (Pisum sativum L.). Planta. 1990;180(2):278-84doi: 10.1007/BF00194008.
Edwards, E. A., Rawsthorne, S., & Mullineaux, P. M. (1990). Subcellular distribution of multiple forms of glutathione reductase in leaves of pea (Pisum sativum L.). Planta, 180(2), 278-84. https://doi.org/10.1007/BF00194008
Edwards, E A, et al. "Subcellular distribution of multiple forms of glutathione reductase in leaves of pea (Pisum sativum L.)." Planta vol. 180,2 (1990): 278-84. doi: https://doi.org/10.1007/BF00194008
Edwards EA, Rawsthorne S, Mullineaux PM. Subcellular distribution of multiple forms of glutathione reductase in leaves of pea (Pisum sativum L.). Planta. 1990 Jan;180(2):278-84. doi: 10.1007/BF00194008. PMID: 24201957.
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Planta. 1990 Jan;180(2):278-84. doi: 10.1007/BF00194008.

Subcellular distribution of multiple forms of glutathione reductase in leaves of pea (Pisum sativum L.).

Planta

E A Edwards, S Rawsthorne, P M Mullineaux

Affiliations

  1. John Innes Institute and AFRC Institute of Plant Science Research, Colney Lane, NR4 7UH, Norwich, UK.

PMID: 24201957 DOI: 10.1007/BF00194008

Abstract

On sodium-dodecyl-sulfate polyacrylamide gels, purified glutathione reductase (GR; EC 1.6.4.2) from the leaves of two- to three-week-old pea (Pisum sativum L. cv. Birte) seedlings was represented by a single band with an apparent molecular weight of 55 kilodaltons. This polypeptide was resolved to multiple isoforms by two-dimensional electrophoresis. Fractionation of protoplasts and purification of subcellular organelles has shown that enzyme activity is associated with the chloroplasts, mitochondria and cytosol (in this order, approx. 77%, 3%, and 20% of the total activity). Distinct multiple isoforms of the enzyme, which differed in isoelectric point and were compartment-specific, were resolved from purified mitochondria and chloroplasts. The latency of the glutathione reductase activity which co-purified on Percoll gradients with the mitochondrial marker enzyme, cytochrome-c oxidase (EC 1.9.3.1.), indicated that this enzyme was within the mitochondrion. The mitochondrial glutathione reductase activity was strongly dependent on NADPH and not NADH.

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