Guikema J A, Sherman L A
Arch Biochem Biophys. 1983 Jan;220(1):155-66. doi: 10.1016/0003-9861(83)90396-x.
Six chlorophyll-containing bands were observed upon electrophoretic analysis of Anacystis nidulans thylakoid membranes. These ranged in apparent molecular weights from approximately 360 to 45 kdalton. Measurements of the light absorption and chlorophyll fluorescence properties of these bands revealed numerous differences among the aggregates. The larger chlorophyll-protein complexes had a chlorophyll absorption maximum at 676 nm while the smallest band, band VI, at approximately 45 kdalton, absorbed at 668 nm. The chlorophyll-protein organization of four submembrane particles was also examined. Digitonin and N-tetradecyl-N,N-dimethyl-3-ammonio-1-pro-panesulfonate were used to fractionate thylakoids and each treatment yielded two green fractions after sucrose density gradient centrifugation. The upper green fractions of both procedures were enriched in band VI. In addition, these fractions showed low temperature fluorescence emission at 686 nm. Conversely, the lower green fractions were enriched in the larger bands (bands I and II), and yielded fluorescence emission at 696 and 716 nm. The gel electrophoresis analysis of these chlorophyll-protein bands revealed 11 peptides ranging in size from less than 10 to 64 kdaltons. The larger CP bands contained as many as five to six polypeptides, whereas band VI contained only two species (at 45 and 48 kdalton). These data suggest that the only proteins in band V (approximately 75 kdalton) and band VI are the chlorophyll binding proteins for photosystems I and II, respectively. We present a model which correlates chlorophyll-protein organization and specific fluorescence emission peaks. Central to this model is the interaction of the larger chlorophyll-protein complexes with bands V and VI to yield fluorescence at 696 and 716 nm, respectively. In addition, the polypeptide composition of each complex allows us to construct a topological model of these complexes within the Anacystis thylakoid.
对集胞藻6803类囊体膜进行电泳分析时观察到了六条含叶绿素的条带。这些条带的表观分子量范围约为360至45千道尔顿。对这些条带的光吸收和叶绿素荧光特性的测量揭示了聚集体之间的许多差异。较大的叶绿素 - 蛋白质复合物在676nm处有叶绿素吸收最大值，而最小的条带，即第六条带，约45千道尔顿，在668nm处吸收。还研究了四个亚膜颗粒的叶绿素 - 蛋白质组织。用洋地黄皂苷和N - 十四烷基 - N，N - 二甲基 - 3 - 铵基 - 1 - 丙烷磺酸盐对类囊体进行分级分离，每种处理在蔗糖密度梯度离心后产生两个绿色级分。两种方法的上层绿色级分都富含第六条带。此外，这些级分在686nm处显示低温荧光发射。相反，下层绿色级分富含较大的条带（第一条带和第二条带），并在696和716nm处产生荧光发射。对这些叶绿素 - 蛋白质条带的凝胶电泳分析揭示了11种肽，大小范围从小于10至64千道尔顿。较大的叶绿素 - 蛋白质条带包含多达五到六种多肽，而第六条带仅包含两种（45和48千道尔顿）。这些数据表明，第五条带（约75千道尔顿）和第六条带中的唯一蛋白质分别是光系统I和II的叶绿素结合蛋白。我们提出了一个将叶绿素 - 蛋白质组织与特定荧光发射峰相关联的模型。该模型的核心是较大的叶绿素 - 蛋白质复合物与第五条带和第六条带的相互作用，分别产生696和716nm处的荧光。此外，每个复合物的多肽组成使我们能够构建集胞藻6803类囊体内这些复合物的拓扑模型。
