Abstract
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.
Publication Date
1-1-1992
Journal Title
Plant Physiology
Digital Object Identifier (DOI)
10.1104/pp.100.2.677
Document Type
Article
Recommended Citation
Stanley P. Kowalski, Nancy T. Eannetta, Alan T. Hirzel & John C. Steffens, "Purification and Characterization of Polyphenol Oxidase from Glandular Trichomes of Solanum Berthaultii," 100 Plant Physiology 677 (1992), available at http://www.plantphysiol.org/content/100/2/677.short
Rights
Copyright American Society of Plant Biologists.