Open AccessReversible chemical cross‐linking of the light‐harvesting polypeptides of Rhodopseudomonas viridis
Author(s) -
LUDWIG Franz Rupert,
JAY Frances Alexandra
Publication year - 1985
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1985.tb09071.x
Subject(s) - reagent , molecular mass , polyacrylamide gel electrophoresis , gel electrophoresis , chemistry , polyacrylamide , beta (programming language) , proton nmr , alpha (finance) , stereochemistry , chromatography , biochemistry , polymer chemistry , organic chemistry , enzyme , medicine , construct validity , nursing , computer science , programming language , patient satisfaction
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 corss‐linking reagents have been characterized using NMR and infrared spectroscopy and thin‐layer chromatography. The cross‐linking reaction was carried out under physiolocigal 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‐α and B1015‐α, between B1015‐α and B1015‐β and B1015‐β. Aggregates of higher molecular mass were hetero‐oligomers of B1015‐α and B1015‐β contaning 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‐α and B1015‐β around the reaction centre core.