Solar Energy Research Group, The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama 351-01, Japan.
Plant Physiol. 1987 Nov;85(3):638-42. doi: 10.1104/pp.85.3.638.
Phosphorylated thylakoid proteins of spinach (Spinacia oleracea L.) and pea (Pisum sativum L.) were solubilized, fractionated by sucrose density gradient centrifugation, and analyzed by gel electrophoresis and crossed immunoelectrophoresis to identify the phosphoproteins. It was found that in addition to intense phosphorylation of light-harvesting chlorophyll complex II, four photosystem II components, CP43 apoprotein, D1, D2, and a 10 to 11 kilodalton protein, are substantially phosphorylated in the light. Furthermore, the CP43 apoprotein, D1 and D2 can be resolved into two electrophoretic subspecies, only one of which is phosphorylated. This indicates that only a fraction of the PSII polypeptides is phosphorylated. Finally, analysis of detergent procedures suggests that the 10 to 11 kilodalton phosphoprotein is a peripheral component of the O(2)-evolving PSII reaction center complex.
菠菜（Spinacia oleracea L.）和豌豆（Pisum sativum L.）的磷酸化类囊体蛋白经蔗糖密度梯度离心分离后，通过凝胶电泳和交叉免疫电泳进行分析，以鉴定磷酸化蛋白。结果发现，除了光捕获叶绿素复合物 II 的强烈磷酸化外，四种光系统 II 组分 CP43 脱辅基蛋白、D1、D2 和 10 到 11 千道尔顿的蛋白质在光照下也大量磷酸化。此外，CP43 脱辅基蛋白、D1 和 D2 可以被解析成两种电泳亚类，只有一种被磷酸化。这表明只有一部分 PSII 多肽被磷酸化。最后，去污剂处理分析表明，10 到 11 千道尔顿的磷酸化蛋白是 O(2)产生 PSII 反应中心复合物的外周成分。
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