COLOCALIZATION OF POLYPHENOL OXIDASE AND PHOTOSYSTEM-II PROTEINS

被引:37
作者
LAX, AR [1 ]
VAUGHN, KC [1 ]
机构
[1] USDA ARS,SO WEED SCI LAB,STONEVILLE,MS 38776
关键词
D O I
10.1104/pp.96.1.26
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Polyphenol oxidase (PPO) appears to be ubiquitous in higher plants but, as yet, no function has been ascribed to it. Herein, we report on the localization of PPO based upon biochemical fractionation of chloroplast membranes in Vicia faba (broad bean) into various complexes and immunocytochemical electron microscopic investigations. Sucrose density gradient fractionations of thylakoid membranes after detergent solubilization reveals that PPO protein (by reactivity with anti-PPO antibody) and activity (based upon ability to oxidize dl-dihydroxyphenylalanine) are found only in fractions enriched in photosystem II (PSII). Furthermore, of the PSII particles isolated using three different protocols utilizing several plant species, all had PPO. Immunogold localization of PPO on thin sections reveals exclusive thylakoid labeling with a distribution pattern consistent with other PSII proteins (80% grana, 20% stroma). These data strongly indicate that PPO is at least peripherally associated with the PSII complex.
引用
收藏
页码:26 / 31
页数:6
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