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Identification of Renibacterium salmoninarum surface proteins by radioiodination
Author(s) -
Fredriksen Åse,
Bakken Vidar
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb07116.x
Subject(s) - polyclonal antibodies , peptide sequence , biochemistry , microbiology and biotechnology , molecular mass , sequence (biology) , biology , bacteria , amino acid , chemistry , sequence analysis , antibody , enzyme , gene , genetics
Surface exposed proteins of Renibacterium salmoninarum were identified by radiolabelling whole bacterial cells with 125 I, 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.

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