Plant cell responses to heavy metals: Molecular and physiological aspects

Acta Physiologiae Plantarum

Volumn 19, Issue 4, 1997, Pages 459-465

  Gwóźdź, Edward A ^a   Przymusiński, Roman ^a   Rucińska, Renata ^a   Deckert, Joanna ^a  

^a ADAM MICKIEWICZ UNIVERSITY   (Poland)

Author keywords

Antioxidant enzymes; Electron paramagnetic resonance; Free radicals; Lead; Pathogen related proteins; Phytochelatins

Indexed keywords

FELIS CATUS; LUPINUS LUTEUS; STAPHYLOCOCCUS PHAGE 187;

EID: 0344352460     PISSN: 01375881     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11738-997-0042-5     Document Type: Conference Paper

References (19)

1. Beauchamp Ch., Fridovich I. 1971. Superoxide dismutase. Improved assays and an assay applicable to acrylamide gel. Anal. Biochem. 44: 276-287.
2. Becana M., Aparci-Tejo P., Irigoyen J. J., Sanchez-Diaz M. 1986. Some enzymes of hydrogen peroxide metabolism in leaves and root nodules of Medicago sativa. Plant Physiol. 82:1160-1171.
3. Breitender H., Pettenburger K., Bito A., Valenta R., Kraft D., Rumpold H., Scheiner O., Breitenbach M. 1989. The gene coding for the major birth pollen allergen Betvl, is highly homologous to a pea disease resistance response gene. EMBO J. 8: 1935-1938.
4. Davis B. J. 1964. Disc electrophoresis-II: method an application to human serum proteins. Ann. of New York Acad. Sci. 121: 404-427.
5. Grill E., Winnacker E.-L., Zenk M. H. 1987 Phytochelatins , a class of heavy-metal-binding peptides from plants , are functionally analogous to metallothoioneins. Proc. Nat. Acad.Sci. USA. 84: 517-524.
6. Harborne J.B. 1989. Introduction to Ecological Biochemistry, Academic Press Harcourt Brace Jovanovich, Publishers.
7. Mittler R., Zilinskas B. A. 1993. Detection of ascorbate peroxidase activity in native gels by inhibition of the ascorbate-dependent reduction of nitroblue tetrazolium. Anal. Bioch. 212, 540-546.
8. Moiseyev G.P., Fedoreyeva L.I., Zhuravlev Y.N., Yasnetskaya E., Jakel P.A., Beintema J.J. 1997. Primary structures of two ribonucleases from ginseng calluses. New members of the PR-10 family of intracellular pathogenesis-related plant proteins. FEBS Lett. 407: 207-210.
9. Pinto M.P., Ricardo C.P.P. 1995. Lupinus albus L. pathogenesis related proteins that show similarity to PR-10 proteins. Plant Physiol., 109: 1345-1352.
10. Przymusiński R., Spychała M., Gwóźdź E. A. 1991. Inorganic lead changes growth and polypeptide pattern of lupin roots. Biochem. Physiol. Pflanzen, 187: 51-57.
11. 3 Mr polypeptide in lupin roots exposed to lead, copper and nitrate ions. Environ. Exp. Bot., 34: 63-68.
12. Przymusiński R., Rucińska R., Gwóźdź E. A. 1995. The stress-stimulated 16kDa polypeptide from lupin roots has properties of cytosolic Cu:Zn-Superoxide dismutase. Environ. Exp. Bot., 35: 485-495.
13. th FESPP Congress, pp.258.
14. Robinson N.J., Urwin P.E., Robinson P.J., Jackson P.J. 1994. Gene expression in relation to metal toxicity and tolerance. In Stress-Induced Gene Expression in Plants, ed. A.S. Basra, Harwood Academic Publisher: 209-248
15. Sikorski M.M., Szlagowska A.E., Legocki A.B. 1995. cDNA sequences encoding for two homologues of Lupinus luteus (L.) IPR-like proteins (Accession No. X79974 and X79975 for LIR18A and LIR18B mRNA=s respectively) Plant Physiol. 110: 335.
16. Tukendorf A., Rauser W. E. 1990. Changes in glutathione and phytochelatins in roots of maize seedlings exposed to cadmium. Plant Sci. 70: 155-166.
17. Vangronsveld J., Clijsters H. 1994. Toxic Effect of Metals. In Plants and the Chemical Elements, ed by M. G. Farago, VCH Weinheim New York Basel Cambridge Tokyo:149-177.
18. Woodbury W., Spencer A. K., Stahmann M. A. 1971. An improved procedure using ferricyanide for detecting catalase isozymes. Analytical Biochemistry, 44: 301-305.
19. Wilkins D.A. 1957. A technique for the measurement of lead tolerance in plants. Nature 180: 37-38.