Tomato Peroxidase: Rapid Isolation and Partial Characterization

ABSTRACT A rapid method for the isolation of tomato anionic peroxidase (TAPR) was developed using Fast Protein Liquid Chromatography. TAPR was purified 295 times to an RZ value of 0.7. The rate constant for the formation of compound I was 1.53 × 10 7 M −1 sec −1 and for compound II was 6.93 × 10 5 M −1 sec −1 . TAPR had maximum activity at pH 5.0–5.2 and an isoelectric point at pH 3.5. SDS gel electrophoresis showed three major bands at 16.6, 40.0, and 42.0 kD. TAPR demonstrated a calcium dependancy for activity, exhibiting a maximum at a concentration of 1.0 × 10 −5 M.