Tomato Peroxidase: Purification by Affinity Chromatography

Abstract

The glycoprotein nature of soluble peroxidase isolated from the tomato fruit was established using Schiff's reagent after periodic oxidation. This enzyme retained on a concanavalin A Sepharose column was eluted using an α-methyl-D-mannoside gradient. On including this step in the purification scheme, the tomato peroxidase was purified 263-fold with a yield of 63%. The enzyme so obtained was homogeneous on polyacrylamide gel electrophoresis and its RZ value was 2.8.