Species and organ diversity in the effects of hydrogen peroxide on superoxide dismutase activity in vitro

Journal of Integrative Plant Biology

Volumn 48, Issue 6, 2006, Pages 672-678

  Cheng, Hong Yan ^a,b   Song, Song Quan ^a  

^a KEY LABORATORY OF TROPICAL FOREST ECOLOGY   (China)

^b INSTITUTE OF BOTANY   (China)

Author keywords

Hydrogen peroxide; In gel assay system; Inhibitor informative; Solution assay system; Species and organ diversity; Superoxide dismutase activity

Indexed keywords

HYDROGEN PEROXIDE; MITOCHONDRION; PLANT; SPECIES DIVERSITY;

ARTOCARPUS HETEROPHYLLUS; GLYCINE MAX; NELUMBO NUCIFERA; TRITICUM AESTIVUM; VIGNA RADIATA VAR. RADIATA; ZEA MAYS;

EID: 33744954046     PISSN: 16729072     EISSN: 17447909     Source Type: Journal    
DOI: 10.1111/j.1744-7909.2006.00266.x     Document Type: Article

References (19)

1. Allen RD (1995). Dissection of oxidative stress tolerance using transgenic plants. Plant Physiol 107, 1049-1054.
2. Apel K, Hirt H (2004). Reactive oxygen species: Metabolism, oxidative stress, and signal transduction. Annu Rev Plant Biol 55, 373-399.
3. Bailly C (2004). Active oxygen species and antioxidants in seed biology. Seed Sci Res 14, 93-107.
4. Beauchamp C, Fridovich I (1971). Superoxide dismutase: Improved assays and an assay applicable to acrylamide gel. Anal Biochem 44, 276-287.
5. Biemelt S, Keetman U, Mock HP, Grimm B (2000). Expression and activity of isoenzymes of superoxide dismutase in wheat roots in response to hypoxia and anoxia. Plant Cell Environ 23, 135-144.
6. Bowler C, van Camp W, Van Montagu M, InzéD (1994). Superoxide dismutase in plants. Crit Rev Plant Sci 13, 199-218.
7. Bradford MM (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding. Anal Biochem 72, 248-254.
8. Douce R (1985). Mitochondria in Higher Plants. Structure, Function, and Biogenesis. Academic Press, New York.
9. Karpinski S, Wingsle G, Karpinska B, Hällgren JE (1993). Molecular response to photooxidative stress in Pinus sylvestris (L.). II. Differential expression of CuZn-superoxide dismutases and glutathione reductase. Plant Physiol 103, 1385-1391.
10. Mackenzie S, Mclntosh L (1999). Higher plant mitochondria. Plant Cell 11, 571-585.
11. Møller IM (2001). Plant mitochondria and oxidative stress: Electron transport, NADPH turnover, and metabolism of reactive oxygen species. Annu Rev Plant Physiol Plant Mol Biol 52, 561-591.
12. Moran JF, James EK, Rubio MC, Sarath G, Klucas RV, Becana M (2003). Functional characterization and expression of a cytosolic ironsuperoxide dismutase from cowpea root nodules. Plant Physiol 133, 773-782.
13. Rasmusson AG, Møller IM (1991). NADP-utilizing enzymes in the matrix of plant mitochondria. Plant Physiol 94, 1012-1018.
14. Rubio MC, Ramos J, Webb KJ, Minchin FR, Gonzalez E, Arrese-Igor C et al. (2001). Expression studies of superoxide dismutases in nodules and leaves of transgenic alfalfa reveal abundance of iron-containing isozymes, posttranslational regulation, and compesation of isozymes activities. Mol Plant-Microbe Interact 14, 1178-1188.
15. Sakamoto A, Okumura T, Kaminaka H, Tanaka K (1995). Molecular cloning of the gene (SodCc1) that encodes a cytosolic copper/zinc-superoxide dismutase from rice (Oryza sativa L.). Plant Physiol 107, 651-652.
16. Scandalios JG (1993). Oxygen stress and superoxide dismutases. Plant Physiol 101, 7-12.
17. Song SQ, Fu JR (1997). Desiccation sensitivity and lipid peroxidation in Chinese wampee (Clausena lansium (Lour.) Skeels) seeds. Acta Phytophysiol Sin 23, 163-168.
18. Song SQ, Berjak P, Pammenter N, Ntuli TM, Fu JR (2003). Seed recalcitrance: A current assessment. Acta Bot Sin 45, 638-643.
19. Struglics A, Fredlund KM, Rasmusson AG, Møller IM (1993). The presence of a short redox chain in the membrane of intact potato tuber peroxisomes and the association of malate dehydrogenase with the peroxisomal membrane. Physiol Plant 88, 19-28.