A cationic peroxidase in leaves of Vitis pseudoreticulata was purified usin
g ion exchange chromatography and on a zeolite column. Characteristics of t
he purified cationic peroxidase were partially analyzed. The results showed
that the cationic peroxidase had a maximum absorbance at ca. 450 nm, a M-r
ca. 39000, and a pi more than 8.0. The optimum catalytic pH value was ca.
5.76, when guaiacol was used as substrate. The apparent T-max and K-m was 6
37 mu mol/mg protein/min and 1.02 mmol/l H2O2 respectively. The peroxidase
was stimulated by high concentrations of inorganic salts. (C) 1999 Elsevier
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