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Identity of Treponema pallidum subsp. pallidum polypeptides: Correlation of sodium dodecyl sulfate‐polyacrylamide gel electrophoresis results from different laboratories
Author(s) -
Norris Steven J.,
Alderete John F.,
Axelsen Nils H.,
Bailey Mark J.,
BakerZander Sharon A.,
Baseman Joel B.,
Bassford Philip J.,
Baughn Robert E.,
Cockayne Alan,
Hanff Philip A.,
Hindersson Peter,
Larsen Sandra A.,
Lovett Michael A.,
Lukehart Sheila A.,
Miller James N.,
Moskophidis Matthäus A.,
Müller Ferdinand,
Norgard Michael V.,
Penn Charles W.,
Stamm Lola V.,
van Embden Jan D.,
Wicher Konrad
Publication year - 1987
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150080202
Subject(s) - treponema , gel electrophoresis , sodium dodecyl sulfate , polyacrylamide gel electrophoresis , microbiology and biotechnology , biology , antiserum , gel electrophoresis of proteins , electrophoresis , biochemistry , chromatography , chemistry , antibody , genetics , virology , enzyme , syphilis , human immunodeficiency virus (hiv)
As the first step in a cooperative effort to standardize the identification of the polypeptides of Treponema pallidum subsp. pallidum , the sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) results obtained in 16 laboratories were compared. Although it was possible to correlate the positions of 16 of the major polypeptide bands, the cross‐identification of many of the polypeptides was ambiguous, particularly in the low molecular weight range. Two‐dimensional electrophoresis provided an improved means of separating and characterizing T. pallidum polypeptides as isolated molecular species. An approach to the unambiguous identification of treponemal polypeptides was outlined which will utilize two‐dimensional electrophoresis in combination with specific properties attributable to individual proteins, including reactivity with monoclonal antibodies or monospecific antisera, biochemical and structural properties, and sequence information. To demonstrate the feasibility of this approach, two‐dimensional electrophoresis in conjunction with immunoperoxidase staining was used to specifically identify three cloned T. pallidum proteins.