Peroxidases are part of a large group of enzymes associated with cell wall biosynthesis, response to injury, disease, resistance and wound repair. Among peroxidase isoenzymes, a soluble cationic peroxidase (ALSP), not yet described, has been partially purified and characterized from artichoke leaves. The enzyme was shown to be a glycoprotein with a molecular weight of 51 000 and an isoelectric point of 9. The substrate specificity of the ALSP is characteristic of class III (guaiacol-type) peroxidases. The ALSP was partially purified by ammonium sulfate precipitation, gel filtration, affinity chromatography, anionic exchange high-performance liquid chromatography and isoelectrofocusing. The increase in specific activity was 43 times compared to the crude extract as estimated by the guaiacol assay. Three ALSP fragments were sequenced by tandem mass spectrometry de novo sequencing method.
Purification and characterization of a cationic peroxidase from artichoke leaves.
LATTANZIO, VINCENZO;
2007-01-01
Abstract
Peroxidases are part of a large group of enzymes associated with cell wall biosynthesis, response to injury, disease, resistance and wound repair. Among peroxidase isoenzymes, a soluble cationic peroxidase (ALSP), not yet described, has been partially purified and characterized from artichoke leaves. The enzyme was shown to be a glycoprotein with a molecular weight of 51 000 and an isoelectric point of 9. The substrate specificity of the ALSP is characteristic of class III (guaiacol-type) peroxidases. The ALSP was partially purified by ammonium sulfate precipitation, gel filtration, affinity chromatography, anionic exchange high-performance liquid chromatography and isoelectrofocusing. The increase in specific activity was 43 times compared to the crude extract as estimated by the guaiacol assay. Three ALSP fragments were sequenced by tandem mass spectrometry de novo sequencing method.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
