Purification of Euphorbia characias latex peroxidase by calmodulin-affinity chromatography.
A new procedure to purify to homogeneity an Euphorbia characias latex peroxidase is performed employing a calmodulin-Sepharose column as affinity chromatography. The advantage of this approach is the isolation of a peroxidase under fast and mild elution conditions with a high recovery in total activity.
Pintus
Francesca
F
Department of Applied Sciences in Biosystems, University of Cagliari, Monserrato, Cagliari, Italy.
Mura
Anna
A
D006631:Amine Oxidase (Copper-Containing) / Q000302:isolation & purification; D000595:Amino Acid Sequence; D002147:Calmodulin / Q000737:chemistry; D002846:Chromatography, Affinity / Q000379:methods*; D028481:Euphorbia / Q000201:enzymology; D007840:Latex / Q000737:chemistry; D008969:Molecular Sequence Data; D009195:Peroxidase / Q000302:isolation & purification*; D012685:Sepharose
D002147:Calmodulin; D007840:Latex; D012685:Sepharose; D009195:Peroxidase; D006631:Amine Oxidase (Copper-Containing)