biologia plantarum

Biologia plantarum 46:111-115, 2003 | DOI: 10.1023/A:1027345318226

Characterization of Polyphenol Oxidase from the Latex of Opium Poppy

F. Bilka¹, A. Balažová¹, A. Bilková¹, Z. Šubr², M. Pšenák¹

¹ Department of Cell and Molecular Biology of Drugs, Faculty of Pharmacy, Comenius University, Bratislava, Slovak Republic

² Institute of Virology, Slovak Academy of Sciences, Bratislava, Slovak Republic

Polyphenol oxidase from the latex of opium poppy was purified to the electrophoretic homogeneity by affinity chromatography using p-aminobenzoic acid as a ligand coupled to Sepharose CL-4B by divinyl sulphone activation method. The purified enzyme was used to prepare the polyclonal antibodies. The purified latex PPO exhibited high diphenolase activity in comparison with almost unmeassurable monophenolase activity. Both of these activities were sensitive to the activation with sodium dodecyl sulphate. Two isoforms (65 and 40 kDa) of latex PPO were separated by the gel filtration. There were no differences in substrate specifity (weak monophenolase and high diphenolase activity) and sensitivity to inhibitors between these isoforms, but they showed differences in electrophoretic mobility.

Keywords: enzyme isoforms; Papaver somniferum

Subjects: latex, polyphenol oxidase; opium poppy, polyphenol oxidase; Papaver somniferum; polyphenol oxidase; poppy, opium, polyphenol oxidase

Published: July 1, 2003  Show citation