A novel extracellular peroxidase and nucleases from a milky sap of Chelidonium majus.
Using affinity chromatography, SDS-PAGE, peroxidase activity assay and mass spectrometry data, a new extracellular peroxidase (CMP) from Chelidonium majus milky sap was isolated and characterized. The protein has a molecular weight of about 40 kDa and belongs to secretory class III plant peroxidases. The peroxidase activity is also accompanied by DN-ase activities. A novel CMP combined with other proteins is probably involved in development and differentiation of the plant and defence against different pathogens. It suggests that the biological activity of C. majus whole plants and extracts may depend not only on its alkaloidal content but also on the presence of biologically active proteins.
Nawrot
Robert
R
Department of Molecular Virology, Institute of Experimental Biology, Adam Mickiewicz University, Umultowska 89, 61-614 Poznan, Poland. rnawrot@amu.edu.pl
Lesniewicz
Krzysztof
K
Pienkowska
Joanna
J
Gozdzicka-Jozefiak
Anna
A
D028281:Chelidonium / Q000737:chemistry* / Q000201:enzymology; D018744:DNA, Plant / Q000032:analysis; D003851:Deoxyribonucleases / Q000737:chemistry; D006801:Humans; D009195:Peroxidase / Q000737:chemistry; D008517:Phytotherapy; D018515:Plant Leaves; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics; D018517:Plant Roots
D018744:DNA, Plant; D010940:Plant Proteins; D009195:Peroxidase; D003851:Deoxyribonucleases