Resolution of Chlorophyll a/b-Protein Complexes by Polyacrylamide Gel Electrophoresis: Evidence for the Heterogeneity of Light-Harvesting Chlorophyll a/b-Protein Complexes
Resolution of Chlorophyll a/b-Protein Complexes by Polyacrylamide Gel Electrophoresis: Evidence for the Heterogeneity of Light-Harvesting Chlorophyll a/b-Protein Complexes
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通过聚丙烯酰胺凝胶电泳分离叶绿素 a/b-蛋白复合物：光捕获叶绿素 a/b-蛋白复合物异质性的证据
DOI：
10.1093/oxfordjournals.pcp.a077448
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发表时间：
1987
影响因子：
4.9
通讯作者：
H. Tsuji
中科院分区：
文献类型：
--
作者：
A. Tanaka;Yoshio Tanaka;H. Tsuji
京都大学理学部植物生态学研究室，日本京都606，用SDS-聚丙烯酰胺凝胶电泳（PAGE）在非变性条件下分离了菠菜类囊体的P700-Chla-蛋白复合物（CP 1和CP 1 *）、PS Ⅱ核心的Chl-蛋白复合物（CP a-1和CP a-2）、捕光Chla/A-蛋白复合物（LHCP o和LHCP m）和CP 29。通过电泳纯化的LHCP寡聚体具有29.5-和27-kDa多肽。利用十二烷基硫酸锂（LDS）聚丙烯酰胺凝胶电泳系统，对菠菜类囊体中的CP 1、CP 29和两个LHCP（LHCP-1和LHCP-2）进行了高分辨电泳分离。两种LHCP在凝胶上显示出相同的吸收光谱。当LHCP低聚物通过该系统再结晶时，它也得到LHCP-1和LHCP-2。LHCP-1具有29.5-和27-kDa多肽，但LHCP-2仅具有29.5 kDa多肽。这两种多肽似乎都能与气结合。在菜豆类囊体中也观察到LHCP的异质性。
Laboratory for Plant Ecological Studies, Faculty of Science, Kyoto University, Kyoto 606, Japan P700-Chl a-protein complexes (CP1 and CP1*), Chl-protein complexes of PS II core (CPa-1 and CPa-2), light-harvesting Chi a/A-protein complexes (LHCPo and LHCPm) and CP29 of spinach thylakoids were resolved by SDS-polyacrylamide-gel electrophoresis (PAGE) under non-denaturing conditions. The LHCP oligomer purified by electrophoresis, had 29.5- and 27-kDa polypeptides. CP1, CP29 and two LHCPs (LHCP-1 and LHCP-2) of spinach thylakoids were separated by a lithium dodecylsulfate (LDS) PAGE system with high resolution. The two LHCPs showed the same absorption spectrum on the gel. When LHCP oligomer was reelectrophoresed by this system it also gave LHCP-1, and LHCP-2. LHCP-1 had both 29.5- and 27- kDa polypeptides, but LHCP-2 had only 29.5 kDa polypeptide. Both polypeptides seemed to bind Chi. The heterogeneity of LHCP was also observed with bean thylakoids.