Immunochemical relationship of the major outer membrane protein of Rhodopseudomonas sphaeroides 2.4.1 to proteins of other photosynthetic bacteria.
Immunoblots of sodium dodecyl sulfate-polyacrylamide gels derived from outer membrane preparations of various strains of Rhodopseudomonas sphaeroides revealed polypeptides which cross-reacted with antibody directed against the major outer membrane protein of R. sphaeroides 2.4.1. Immunochemical quantitation of the major outer membrane protein of strain 2.4.1 showed approximately 5.5 x 10(4) molecules per cell whether cells were grown chemoheterotrophically or photoheterotrophically. Rhodospirillum rubrum outer membranes contained a cross-reactive protein, whereas the outer membranes derived from Rhodopseudomonas capsulata and Paracoccus denitrificans showed no cross-reaction with the antibody prepared against the major outer membrane protein from R. sphaeroides 2.4.1.
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins / Q000276:immunology*; D003378:Counterimmunoelectrophoresis; D003429:Cross Reactions; D000939:Epitopes / Q000032:analysis; D008565:Membrane Proteins / Q000276:immunology*; D010231:Paracoccus denitrificans / Q000276:immunology; D010788:Photosynthesis; D012242:Rhodobacter sphaeroides / Q000276:immunology* / Q000502:physiology; D012241:Rhodopseudomonas / Q000276:immunology; D012246:Rhodospirillum / Q000276:immunology; D013045:Species Specificity
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D000939:Epitopes; D008565:Membrane Proteins