Oligomerization states and associations of light-harvesting pigment-protein complexes of Rhodobacter sphaeroides as analyzed by lithium dodecyl sulfate-polyacrylamide gel electrophoresis

• Published in: Biochemistry (Easton) 1988-05, Vol.27 (9), p.3459-3467
• Main Authors: Hunter, C. Neil, Pennoyer, Jeffrey D, Sturgis, James N, Farrelly, Dennis, Niederman, Robert A
• Format: Article
• Language: English
• Subjects: Biological and medical sciences; Cell structures and functions; Chloroplast, photosynthetic membrane and photosynthesis; Fundamental and applied biological sciences. Psychology; Molecular and cellular biology; Rhodobacter sphaeroides
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi00409a050

The stability and migration behavior of bacteriochlorophyll a-carotenoid-protein complexes of Rhodobacter (formerly Rhodopseudomonas ) sphaeroides in lithium dodecyl sulfate-polyacrylamide gel electrophoresis at 4 degree C were examined. Yields of peripheral B800-850 and core B875 light-harvesting complexes of up to 57% and 15%, respectively, were obtained. Only B875 migrated ideally in gels of different acrylamide concentrations, and estimates of molecular weight suggested an ( alpha beta ) sub(3) structure. In mutant strain NF57, which lacks B875 and reaction centers, only bands in the position of higher B800-850 oligomers were observed. Strain M21, which lacks B800-850, yielded B875 and reaction center bands and an oligomeric series of B875 bands, which comigrated with bands of the wild type that contain the B800-850 and B875 complexes in various associations.