PURIFICATION AND CHARACTERIZATION OF POLYPHENOL OXIDASE FROM GLANDULAR TRICHOMES OF SOLANUM-BERTHAULTII

被引:89
|
作者
KOWALSKI, SP [1 ]
EANNETTA, NT [1 ]
HIRZEL, AT [1 ]
STEFFENS, JC [1 ]
机构
[1] CORNELL UNIV,DEPT PLANT BREEDING & BIOMET,252 EMERSON HALL,ITHACA,NY 14853
关键词
D O I
10.1104/pp.100.2.677
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Type A glandular trichomes of the wild potato (Soianum 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 mum 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.
引用
收藏
页码:677 / 684
页数:8
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