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Comparative Study
. 1999 Jan;6(1):146-8.
doi: 10.1128/CDLI.6.1.146-148.1999.

Specificity of the 34-kilodalton immunodominant protein of Mycobacterium avium sp. paratuberculosis

P Gilot
Comparative Study

Specificity of the 34-kilodalton immunodominant protein of Mycobacterium avium sp. paratuberculosis

P Gilot. Clin Diagn Lab Immunol. 1999 Jan.
No abstract available

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Figures

FIG. 1
FIG. 1
Alignment of the amino acid sequences of the 34-kDa protein of M. avium subsp. paratuberculosis (M.para) and of the Rv0954 protein of M. tuberculosis H37Rv (M.tube). The two homologous proteins were aligned by using the Align program (http://vega.igh.cnrs.fr/bin/align-guess.cgi). Black background indicates regions containing identical amino acids. Arrows indicate locations of potential transmembrane helices as predicted by the TMpred program (http://www.isrec.isb-sib.ch/software/TMPRED_form.html). The sequence corresponding to the a362 peptide is boxed.
FIG. 1-1
FIG. 1-1
Analysis by Western blotting of anti-a362 polyclonal serum and Lo-ptb(a362)-4 monoclonal antibody. Soluble sonic extracts (50 μg of protein per sample) of M. avium subsp. paratuberculosis (lanes A and B) and M. bovis (lanes A′ and B′) were fractionated by sodium dodecyl sulfate–12% polyacrylamide gel electrophoresis, transferred to a nitrocellulose membrane, and reacted with either anti-a362 polyclonal serum (lanes A and A′) as described in our paper or anti-a362 monoclonal antibody Lo-ptb(a362)-4 (lanes B and B′). Antigen-antibody complexes were revealed by peroxidase-labelled secondary antibodies as described in our paper.
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