REVERSIBLE CHEMICAL CROSS-LINKING OF THE LIGHT-HARVESTING POLYPEPTIDES OF RHODOPSEUDOMONAS-VIRIDIS
REVERSIBLE CHEMICAL CROSS-LINKING OF THE LIGHT-HARVESTING POLYPEPTIDES OF RHODOPSEUDOMONAS-VIRIDIS
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DOI：
10.1111/j.1432-1033.1985.tb09071.x
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发表时间：
1985-01-01
期刊：
影响因子：
--
通讯作者：
JAY, FA
中科院分区：
文献类型：
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作者：
LUDWIG, FR;JAY, FA
利用可裂解的化学交联剂研究了红球藻捕光多肽的形貌。为此，合成了一组不同跨度宽度的琥珀酰亚胺酯和表面特异性磺基琥珀酰亚胺酯。交联剂的特征在于使用NMR和红外光谱和薄层色谱法。在生理条件下进行交联反应，并通过一维和二维聚丙烯酰胺凝胶电泳和免疫印迹分析的方法进行分析的聚集体。我们发现B1015-α之间的交联。和B1015-β，在B1015-α之间。和B1015-β。和B1015-β。和B1015-β。较高分子量的聚集体是B1015-α的杂寡聚体。和B1015-β。分别含有三种和四种多肽。在这项工作中获得的结果表明，一个非常紧密的联系之间的捕光多肽。我们假设捕光多肽交替地定位为B1015-α的二聚体。和B1015-β。围绕着反应中心的核心
The topography of the light-harvesting polypeptides of Rhodopseudomonas viridis was investigated using cleavable chemical cross-linkers. To this end a set of succinimidyl esters and surface-specific sulfosuccinimidyl esters of different span widths were synthesized. The cross-linking reagents have been characterized using NMR and infrared spectroscopy and thin-layer chromatography. The cross-linking reaction was carried out under physiological conditions and the aggregates were analyzed by the methods of one- and two-dimensional polyacrylamide gel electrophoresis and by immunoblot analysis. We found cross-linkage between B1015-.alpha. and B1015-.beta., between B1015-.alpha. and B1015-.beta. and B1015-.beta. and B1015-.beta.. Aggregates of higher molecular mass were hetero-oligomers of B1015-.alpha. and B1015-.beta. containing three and four polypeptides, respectively. The results obtained in this work indicate a very tight contact among the light-harvesting polypeptides. We assume that the light-harvesting polypeptides are localized alternately as dimers of B1015-.alpha. and B1015-.beta. around the reaction centre core.