Mouse Ficolin B Has an Ability to Form Complexes with Mannose-Binding Lectin-Associated Serine Proteases  and Activate Complement through the Lectin Pathway

<table>Structural characterization of rFcnB. (a) Left panel: Western blot of rFcnB and rFcnBs2-1 treated with endoglycosidase F (endoF). Right panel: western blot of rFcnB and rFcnBs2-1 treated with neuraminidase (neu) or neuraminidase plus endo-<i>α</i>-<i>N</i>-acetylgalactosaminidase (<i>o</i>-gly). Western blotting was performed under reducing conditions. —, not treated. (b) Gel chromatography of rFcnB (upper panel) and rFcnBs2-1 (lower panel). rFcnB or rFcnBs2-1 (400 <i>μ</i>L; 5–10 <i>μ</i>g) was applied to a Superose 6 column (1 cm <i>ϕ</i> × 30 cm) and fractionated into 0.5 mL/fractions. An aliquot of each fraction was subjected to western blotting for FcnB under reducing conditions.</table>

BioMed Research International

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Figure 3

Figure 3: Mouse Ficolin B Has an Ability to Form Complexes with Mannose-Binding Lectin-Associated Serine Proteases  and Activate Complement through the Lectin Pathway 

Figure 3 | Mouse Ficolin B Has an Ability to Form Complexes with Mannose-Binding Lectin-Associated Serine Proteases  and Activate Complement through the Lectin Pathway 