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Plant Physiology 100:677-684 (1992)
© 1992 American Society of Plant Biologists

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Metabolism and Enzymology

Purification and Characterization of Polyphenol Oxidase from Glandular Trichomes of Solanum berthaultii1

Stanley P. Kowalski, Nancy T. Eannetta, Alan T. Hirzel and John C. Steffens

Department of Plant Breeding and Biometry, 252 Emerson Hall, Cornell University, Ithaca, New York 14853

Type A glandular trichomes of the wild potato (Solanum berthaultii Hawkes) entrap insects by rapidly polymerizing the trichome contents after breakage by insect contact. Polymerization of trichome exudate appears to be driven by a soluble polyphenol oxidase (PPO). PPO constitutes up to 70% of the protein in individually collected trichomes and reaches a concentration approaching 200 µM in these organs. Trichome PPO has been purified and shown to be a monomeric copper metalloprotein with an isoelectric point of 5.5, possessing only o-diphenol oxygen oxido-reductase activity, and is larger than most other reported PPOs, with relative molecular weight of 59,000. Chlorogenic and caffeic acid were the most readily oxidized of 14 phenolic substrates tested. Polyclonal antibodies raised against the relative molecular weight 59,000 S. berthaultii trichome PPO were used to show that S. tuberosum L. trichomes express low levels of a cross-reactive protein that lacks detectable PPO activity.

1 This work was supported in part by Hatch Project NYS 149417, the International Potato Center, and by a grant from the Cornell Biotechnology Program, which is sponsored by the New York State Science and Technology Foundation, a consortium of industries, the U.S. Army Research Office, and the National Science Foundation.




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Copyright © 1992 by the American Society of Plant Biologists