Selective solubilization of chlorosome proteins in Chloroflexus aurantiacus.
Proteins were solubilized selectively from chlorosomes of Chloroflexus aurantiacus by electrophoretic gel filtration according to Griebenow et al. Whereas the 11 kDa and 18 kDa proteins were extracted almost completely, the remaining modified chlorosomes contained high amounts of pigment and c-protein. It was concluded that the c-protein in contradiction to the publication by Griebenow et al. is indeed localized in the interior of Chloroflexus chlorosomes.
Institut für Molekularbiologie und Biophysik, ETH-Hönggerberg, Zürich, Switzerland.
A
A
Eckhardt
R
R
Brunisholz
G
G
Frank
H
H
Zuber
D001419:Bacteria / Q000032:analysis*; D001426:Bacterial Proteins / Q000032:analysis*; D001429:Bacteriochlorophylls / Q000032:analysis*; D002734:Chlorophyll / Q000031:analogs & derivatives*; D002850:Chromatography, Gel; D004586:Electrophoresis / Q000379:methods; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D012995:Solubility; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D001429:Bacteriochlorophylls; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D002734:Chlorophyll