Identification of Renibacterium salmoninarum surface proteins by radioiodination.
Surface exposed proteins of Renibacterium salmoninarum were identified by radiolabelling whole bacterial cells with 125I, followed by SDS-PAGE and autoradiography. The most prominent bands had molecular masses of approximately 57 kDa and 22 kDa; in addition, some less intensively labelled bands were detected. Polyclonal sera raised against the 22 kDa protein did not react with the 57 kDa protein. N-terminal amino acid sequence analysis of the purified 22 kDa protein showed no similarity with the sequence of the 57 kDa protein.
Fredriksen
A
A
Department of Fisheries and Marine Biology, Bergen High Technology Center, Norway.
Bakken
V
V
D000595:Amino Acid Sequence; D000818:Animals; D000907:Antibodies, Bacterial; D000942:Antigens, Bacterial / Q000235:genetics / Q000302:isolation & purification; D001426:Bacterial Proteins / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification*; D005393:Fish Diseases / Q000382:microbiology; D006094:Gram-Positive Bacteria / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D016908:Gram-Positive Bacterial Infections / Q000382:microbiology / Q000662:veterinary; D007457:Iodine Radioisotopes; D008565:Membrane Proteins / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012487:Salmonidae / Q000382:microbiology
D000907:Antibodies, Bacterial; D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D007457:Iodine Radioisotopes; D008565:Membrane Proteins