A novel extracellular peroxidase and nucleases from a milky sap of Chelidonium majus

• Published in: Fitoterapia Vol. 78; no. 7; pp. 496 - 501
• Main Authors: Nawrot, Robert, Lesniewicz, Krzysztof, Pienkowska, Joanna, Gozdzicka-Jozefiak, Anna
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 01.12.2007; Elsevier
• Subjects: Biological and medical sciences; Chelidonium - chemistry; Chelidonium - enzymology; Chelidonium majus; Deoxyribonucleases - chemistry; DNA, Plant - analysis; General pharmacology; Humans; Medical sciences; Nuclease; Peroxidase; Peroxidase - chemistry; Pharmacognosy. Homeopathy. Health food; Pharmacology. Drug treatments; Phytotherapy; Plant Leaves; Plant Proteins - chemistry; Plant Proteins - genetics; Plant Roots; Chelidonium majus; Peroxidase; Nuclease; Sap; Enzyme; Pharmacognosy; Esterases; Papaveraceae; Medicinal plant; Peroxidases; Dicotyledones; Angiospermae; Plant origin; Hydrolases; Spermatophyta; Oxidoreductases
• ISSN: 0367-326X
• DOI: 10.1016/j.fitote.2007.04.012

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.