Open AccessCharacterization of PPD protein antigens in whole cell lysates of Mycobacterium bovis BCG
Author(s) -
Bardarov S.S.,
Kriakov J.,
Karakahyan A.,
Sirakova T.D.,
Markov K.
Publication year - 1990
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.1574-6968.1990.tb03803.x
Subject(s) - molecular mass , antiserum , polyclonal antibodies , antigen , mycobacterium bovis , microbiology and biotechnology , chemistry , polyacrylamide gel electrophoresis , gel electrophoresis , epitope , biology , biochemistry , mycobacterium tuberculosis , tuberculosis , enzyme , immunology , medicine , pathology
The low molecular mass protein antigens in PPD from M. bovis BCG were chemically oligomerized using sulfosuccinimidyl‐4‐(p‐maleimidophenyl)‐butyrate (S‐SMPB) as a crosslinking agent. Protein oligomers with molecular mass over 90 kDa were obtained and used for the preparation of hyperimmune polyclonal rabbit antiserum. Using this antiserum four protein bands with molecular mass 120, 90, 75 and 65 kDA were detected in immunoblotting analysis of sonic extract from M. bovis BCG separated in SDS‐polyacrylamide gel. We suggest that these immunoreactive proteins in the sonic extract represent the native forms of the heat stable low molecular mass protein antigens in PPD.