[Isolation and characterization of pigment-protein complexes from green serobacteria Chlorobium limicola forma thiosulfatophilum].

A subchromatophore fraction containing the reaction center P-840 was isolated from the chromatophores of green serobacteria Chlorobium limicola forma thiosulfatophilum by ultracentrifugation and its protein composition was characterized. After treatment of the chromatophores by Triton X-100 and subsequent polyacrylamide gel electrophoresis two pigment-protein complex containing bacterioviridin. The proteins of the pigment-protein complex containing bacterioviridin. The proteins of the pigment-protein complexes were obtained. The first complex contained mainly bacteriochlorophyll alpha with bacterioviridin contaminations and the second one-only bacterioviridin. The low-temperature absorption spectrum of the bacteriochlorophyll alpha-containing pigment-protein complex is identical to the absorption spectrum of a water-soluble pigment-protein complex isolated and characterized by Olson and contains proteins with molecular weights of 34.800, 33.100, 27.500 and 23.200. A protein with molecular weight of 32.700 was found in the pigment-protein complexes were compared to the proteins of the photochemically active subchromatophore fraction and chromatophores.