Separation of horseradish peroxidase isoenzymes by preparative polyacrylamide gel electrophoresis

Abstract

Seven peroxidase isoenzymes were purified from crude horseradish peroxidase (EC 1.11.1.7) (HRP) in a single step by preparative polyacrylamide gel electrophoresis. The peroxidase activity in seven isoenzymes accounted for 90% of the activity in the crude material. Each isoenzyme (except HRP7) after separation migrated as a single band with characteristic electrophoretic mobility. All of the purified isoenzymes were found to retain complete peroxidase activity after storage at −20 °C or 4 °C for 3 months.