Arnon DI: Copper enymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris. Plant Physiol 24: 1–15 (1949).

Google Scholar 

Badger M, Andrews TJ, Canvin DT, Lorimer GH: Interactions of hydrogen peroxide with ribulose bisphosphate carboxylase oxygenase. J Biol Chem 255: 7870–7875 (1980).

PubMed  Google Scholar 

Bartlett SG, Grossman AR, Chua N-H: In vitro synthesis and uptake of cytoplasmically-synthesized chloroplast proteins In: Edelman M et al. (eds) Methods in Chloroplast Molecular Biology, pp. 1081–1091. Elsevier, Amsterdam (1982).

Google Scholar 

Baum JA, Scandalios JG: Developmental expression and intracellular localization superoxide dismutases in maize. Differentiation 13: 133–140 (1979).

Google Scholar 

Baum JA, Chandlee JM, Scandalios JG: Purification and partial characterization of a genetically-defined superoxide dismutase (SOD-1) associated with maize chloroplasts. Plant Physiol: 73: 31–35 (1983).

Google Scholar 

Bjorkman O: Low-temperature chlorophyll fluorescence in leaves and its relationship to photon yield of photosynthesis in photoinhibition. In: Kyle DJ, Osmond CB, Arntzen CJ (eds) Photoinhibition, pp. 123–144. Elsevier Science Publishers (Biomedical Division), Amsterdam/New York/Oxford.

Bowler C, Alliotte T, DeLoose M, VanMontagu M, Inze D: The induction of manganese superoxide dismutase in response to stress in Nicotiana plumbaginifolia. EMBO J 8: 31–38 (1989).

PubMed  Google Scholar 

Bradford MM: 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).

Article  PubMed  Google Scholar 

Cannon RE, White JA, Scandalio JG: Cloning of cDNA for maize superoxide dismutase 2 (SOD2). Proc Natl Acad Sci USA 84: 170–183 (1987).

PubMed  Google Scholar 

Dean C, van denElzen P, Tamaki S, Dunsmuir P, Bedbrook J: Differential expression of the eight genes of the petunia ribulose bisphosphate carboxylase small subunit multi-gene family. EMBO J 4: 3055–3061 (1985).

Google Scholar 

Dean C, Favreau M, Dunsmuir P, Bedbrook J: Confirmation of the relative expression levels of the Petunia (Mitchell) rbcS genes. Nucl Acids Res 15: 4655–4668 (1987).

PubMed  Google Scholar 

Dean C, Favreau M, Tamaki S, Jones J, Dunsmuir P, Bedbrook J: Expression of Petunia rbcS gene fusions in transformed tobacco plants. In: Key J, McIntosh L (eds) Plant Gene Systems and their Biology, pp. 289–295 (1987)

Dean C, Favreau M, Tamaki S, Bond-Nutter D, Dunsmuir P, Bedbrook J: Expression of tandem gene fusions in transgenic tobacco plants. Nucl Acids Res 16: 9267–9283 (1988).

PubMed  Google Scholar 

Elstner EF: Oxygen activation and oxygen toxicity. Ann Rev Plant Physiol 33: 73–96 (1982).

Article  Google Scholar 

Figurski D, Helinski DR: Replication of an origincontaining derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proc Natl Acad Sci USA 76: 1648–1652 (1979).

PubMed  Google Scholar 

Foster JG, Edwards GE: Localization of superoxide dismutase in leaves of C₃ and C₄ plants. Plant & Cell Physiol 21: 895–906 (1980).

Google Scholar 

Foyer CH, Halliwell B: The presence of glutathione and glutathione reductase in chloroplasts. A proposed role in ascorbic acid metabolism. Planta 133: 21–25 (1976).

Google Scholar 

Fridovich I: The biology of oxygen radicals. Science 201: 875–880 (1978).

PubMed  Google Scholar 

Gamon JA, Pearcy RW: Leaf movement stress avoidance and photosynthesis in Vitis californica. Oecologia 79: 475–481 (1989).

Google Scholar 

Halliwell B: The toxic effect of oxygen on plant tissues. In: Oberley LW et al., Superoxide Dismutase, vol. I pp. 89–123 CRC Boca Raton, FL (1982).

Google Scholar 

Hoekema A, Hirsch PR, Hooykaas PJJ, Schilperoort RA: A binary plant vector strategy based on separation of vir-and T-region of the Agrobacterium tumefaciens Ti-plasmid. Nature 303: 179–180 (1983).

Google Scholar 

Horsch RB, Fry JE, Hoffman NL, Wallroth M, Eichkoltz D, Rogers SG, Fraley RT: A simple and general method for transferring genes into plants. Science 227: 1229–1231 (1985).

Google Scholar 

Jones J, Dean C, Gidoni D, Gilbert D, Bond-Nutter D, Lee R, Bedbrook J, Dunsmuir P: High level expression of a bacterial chitinase protein in leaves of transgenic tobacco plants. Mol Gen Genet 212: 536–542 (1988).

Article  Google Scholar 

Kitagawa Y, Tsunasawa S, Tanaka N, Katsube Y, Sakiyama F, Asada K: Amino acid sequence of copper, Zinc-superoxide dismutase from spinach leaves. J Biochem 99: 1289–1298 (1986).

PubMed  Google Scholar 

Kunkel TA: Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc Natl Acad Sci USA 82: 488–492 (1985).

PubMed  Google Scholar 

Lee EH, Bennett JH: Superoxide Dismutase. A possible protective enzyme against ozone injury in snap beans (Phaseolus vulgaris L.) Plant Physiol 69: 1444–1449 (1982).

Google Scholar 

Maniatis T, Fritsch EF, Sambrook J: Molecular Cloning: A Laboratory Manual Cold Spring Harbor Laboratory, Cold Spring Harbor, NY (1982).

Google Scholar 

Moll BA: Flash-induced fluorescence estimation of Photosystem II electron-transport rates in light-adapted leaves. Biochim Biophys Acta 890: 205–214 (1987).

Google Scholar 

Perl-Treves R, Nacmias B, Aviv D, Zeelon EP, Galun E: Isolation of two cDNA clones from tomato containing two different superoxide dismutase sequences. Plant Mol Biol 11: 609–623 (1988).

Google Scholar 

Powles SB, Berry JA, Bjorkman O: Interaction between light and chilling temperature on the inhibition of photosynthesis in chilling-sensitive plants. Plant Cell Envir 6: 117–123 (1983).

Google Scholar 

Rabinowitch HD, Fridovich I: Superoxide radicals, superoxide dismutase and oxygen toxicity in plants. Rev Photochem Photobiol 37: 679–690 (1983).

Google Scholar 

Rabinowitch HD, Sklan D: Superoxide dismutase; a possible protective agent against sunscald in tomatoes (Lycopersicon esculentum Mill.) Planta 148: 162–167 (1980).

Google Scholar 

Scandalios G: Multiple genes controlling superoxide dismutase expression in maize. J Hered 73: 95–100 (1982).

Google Scholar 

Scioli JR, Zilinskas BA: Cloning and characterization of a cDNA encoding the chloroplastic copper/zinc-super-oxide dismutase from pea. Proc Natl Acad Sci USA 85: 7661–7665 (1988).

PubMed  Google Scholar 

Shaaltiel Y, Chua N-H, Gepstein S, Gressel J: Dominant pleiotropy controls enzymes co-segregating with paraquat resistance in Conyza bonariensis. Theor Appl Genet 75: 850–856 (1988).

Google Scholar 

Shaaltiel Y, Gressel J: Multienzyme oxygen radical detoxifying system correlated with paraquat resistance in Conyza bonariensis. Pesticide Biochem and Physiol 26: 22–28 (1986).

Google Scholar 

Tanaka K, Sugahara K: Role of superoxide in defense against SO₂ toxicity and an increase in superoxide dismutase activity with SO₂ fumigation. Plant & Cell Physiol 21: 601–611 (1980).

Google Scholar 

Taylor JL, Jones JDG, Sandler S, Mueller GM, Bedbrook J, Dunsmuir P: Optimizing the expression of chimeric genes in plant cells. Mol Gen Genet 210: 572–577 (1987).

Article  Google Scholar 

Tepperman J, Katayama C, Dunsmuir P: Cloning and nucleotide sequence of a petunia gene encoding a chloroplast localized superoxide dismutase. Plant Mol Biol 11: 871–872 (1988).

Google Scholar 

Vallejos E: Enzyme activity staining. In: Isozymes in Plant Genetics and Breeding, Part 1, pp. 469–516. Elsevier, Amsterdam (1983).

Google Scholar 

Wise RR, Naylor AW: Chilling-enhanced photo-oxidation. Plant Physiol 83: 272–277 (1977).

Google Scholar 

Youngman RJ, Dodge AD: On the mechanism of paraquat resistance in Conyza sp. In: Akoyunoglou G (ed) Photosynthesis, V1. Photosynthesis and Productivity Photosynthesis and Environment, pp. 537–543. Balaban International Services, Philadelphia, PA (1981).

Google Scholar