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. Author manuscript; available in PMC: 2009 Apr 8.
Published in final edited form as: Microbiology (Reading). 2006 Dec;152(Pt 12):3777–3786. doi: 10.1099/mic.0.29162-0

Fig. 4.

Fig. 4

Immunoprecipitation of LipL41 and LipL46 on the surface of L. kirschneri. Total L. kirschneri proteins (lane 1), and proteins immunoprecipitated by antiserum to L. kirschneri after (lane 2) and before (lane 3) solubilization with Triton X-100, were separated by SDS-PAGE, and probed with LipL36, LipL41 and LipL46 antisera. Both LipL41 and LipL46 were found to be present in the surface-immunoprecipitated material. Although LipL36 was immunoprecipitated by the antiserum after solubilization by Triton X-100, it was not accessible to antibody on the surface of L. kirschneri. The locations of the molecular size (kDa) standards are shown on the left.