Biologia plantarum 45:145-147, 2002 | DOI: 10.1023/A:1015145818294

Identification and Analysis of Proteins Sharing Dehydroascorbate Reductase Activity

M.C. De Tullio1, C. Paciolla1, O. Arrigoni1
1 Dipartimento di Biologia e Patologia Vegetale, Università di Bari, Bari, Italia

Dehydroascorbate (DHA)-reducing proteins were observed using a native-PAGE/activity staining method, and identified in soybean and rice by Western analysis using antibodies against homologous protein known to catalyse DHA reduction. Administration of 1 mM DHA apparently did not trigger DHA reductase activity in lupin and onion, whereas activity was increased in rice and barley.

Keywords: Allium cepa; ascorbate regeneration; Glycine max; Lupinus albus; Oryza sativa
Subjects: Allium cepa; barley, dehydroascorbate-reducing proteins; dehydroascorbate reductase; Glycine max; lupin, dehydroascorbate-reducing proteins; Lupinus albus; onion, dehydroascorbate-reducing proteins; Oryza sativa; rice, dehydroascorbate-reducing proteins; soybean, dehydroascorbate-reducing proteins

Published: March 1, 2002Show citation

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Tullio, M.C., Paciolla, C., & Arrigoni, O. (2002). Identification and Analysis of Proteins Sharing Dehydroascorbate Reductase Activity. Biologia plantarum, 45(1), 145-147. doi: 10.1023/A:1015145818294.
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    References

    1. Bradford, M.M.: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.-Anal. Biochem. 72: 248-254, 1976. Go to original source...
    2. De Tullio, M.C., De Gara, L., Paciolla, C., Arrigoni, O.: Dehydroascorbate-reducing proteins in maize are induced by the ascorbate biosynthesis inhibitor lycorine.-Plant Physiol. Biochem. 36: 433-440, 1998. Go to original source...
    3. De Tullio, M.C., Arrigoni, O.: Ascorbic acid and plants: multiple roles and new perspectives-Curr. Topics Phytochem. 2: 135-143, 1999.
    4. Harlow, E., Lane, D.: Antibodies: a Laboratory Manual.-Cold Spring Harbor Laboratory Press, Cold Spring Harbor 1988.
    5. Kato, Y., Urano, J., Maki, Y., Ushimaru, T.: Purification and characterization of dehydroascorbate reductase from rice.-Plant Cell Physiol. 38: 173-178, 1997. Go to original source...
    6. Shimaoka, T., Yokota, A., Miyake, C.: Purification and characterization of chloroplast dehydroascorbate reductase from spinach leaves.-Plant Cell Physiol. 41: 1110-1118, 2000. Go to original source...
    7. Urano, J., Nakagawa, T., Maki, Y., Masumura, T., Tanaka, K., Murata, N., Ushimaru, T.: Molecular cloning and characterization of a rice dehydroascorbate reductase.-FEBS Lett. 466: 107-111, 2000. Go to original source...
    8. Vethanayagam, J.G., Green, E.H., Rose, R.C., Bode, A.M.: Glutathione-dependent ascorbate recycling activity of rat serum albumin.-Free Radical Biol. Med. 26: 1591-1598, 1999.
    9. Washburn, M.P., Wells, W.W.: Identification of the dehydroascorbic acid reductase and thioltransferase (glutaredoxin) activities of bovine erythrocyte glutathione peroxidase.-Biochem. biophys. Res. Commun. 257: 567-571, 1999. Go to original source...

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