[Purification of Meerrettich-peroxidase by means of affinity chromatography on concanavalin A-agarose].
Crude preparations of horse-radish peroxidase were purified by means of affinity chromatography on Concanavalin A-agarose. The peroxydase was bound to Concanavalin A, whereas the majority of other proteins of the preparation pass through the column. Subsequently the peroxidase was eluted by means of 1 M sucrose with high purity. The purified enzyme is convenient for the immunoenzyme technique.
D002021:Buffers; D002846:Chromatography, Affinity; D003208:Concanavalin A; D010544:Peroxidases / Q000302:isolation & purification*; D011134:Polysaccharides; D012685:Sepharose
D002021:Buffers; D011134:Polysaccharides; D003208:Concanavalin A; D012685:Sepharose; D010544:Peroxidases
Reinigung von Meerrettich-Peroxydase durch Affinitätschromatographie an Concanavalin A-Agarose