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Analysis of Major Surface Polypeptides of Rickettsia japonica
Author(s) -
Uchiyama Tsuneo,
Uchida Takahiro,
Walker David H.
Publication year - 1994
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1994.tb01825.x
Subject(s) - gel electrophoresis , biology , polyacrylamide gel electrophoresis , sodium dodecyl sulfate , electrophoresis , biochemistry , denaturation (fissile materials) , sodium , peptide , microbiology and biotechnology , chemistry , enzyme , organic chemistry , nuclear chemistry
Major surface polypeptides of Rickettsia japonica migrated to the position of 120, 135, and 145 kDa on sodium dodecyl sulfate‐polyacrylamide gel electrophoresis, when the organisms were solubilized at room temperature. Two major bands at the position of 135 and 185 kDa were seen, when the organisms were solubilized by heating before electrophoresis. Heat‐denaturation of the 120‐ and 145‐kDa polypeptides in excised gel bands changed their mobility and caused them to migrate to 135‐ and 185‐kDa positions, respectively. Two polypeptides at the 120‐kDa position were demonstrated: one is a major heat‐modifiable polypeptide and the other a minor heat‐stable. Peptide mapping was performed to determine the identity between native and denatured polypeptides.