LIGHT-HARVESTING CHLOROPHYLL-A/B-PROTEINS (LHCII) POPULATIONS IN PHOSPHORYLATED MEMBRANES

LIGHT-HARVESTING CHLOROPHYLL-A/B-PROTEINS (LHCII) POPULATIONS IN PHOSPHORYLATED MEMBRANES
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DOI:
10.1016/0005-2728(88)90248-4
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发表时间:
1988-10-26
期刊:
BIOCHIMICA ET BIOPHYSICA ACTA
影响因子:
--
通讯作者:
GIACOMETTI, GM
GIACOMETTI, GM
中科院分区:
其他
文献类型:
--
作者:
BASSI, R;RIGONI, F;GIACOMETTI, GM

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本文分析了光系统II的光收集叶绿素a/b蛋白复合物(LHCII)磷酸化后在类囊体和PS II膜中的特性。采用一种新开发的分离方法,在颗粒状凝胶中平板电聚焦,从类囊体中分离出7个Chl a/b蛋白。对它们的磷酸化水平和多肽组成进行了评价。在类囊体中,PhosphoLHCII仅占总Chl a/b蛋白的30%,而“可移动”的部分结合了总LHCII叶绿素的20%。紧密结合的LHCII与流动组分的不同之处在于存在一个26 kDa的多肽,其特征是缺乏在状态转变过程中磷酸化的n端LHCII蛋白水解片段。
The properties of the light-harvesting chlorophyll a/b-protein complex of Photosystem II (LHCII) have been analyzed, in thylakoids and PS II membrane after phosphorylation. Using a newly developed fractionation method, by flat-bed electrofocusing in granulated gel, seven Chl a/b proteins have been separated from thylakoids. Their phosphorylation level and polypeptide composition have been evaluated. PhosphoLHCII represent only 30% of the total Chl a/b proteins in thylakoids and the ''mobile'' fraction binds 20% of the total LHCII chlorophyll. Tightly bound LHCII differs from the mobile fraction for the presence of a 26 kDa polypeptide characterized by the absence of the N-terminal LHCII proteolytic fragment which is phosphorylated during state transition.