American Society of Hematology

Fig. 3.

$Fig. 3. The 2-DE of the soluble and membrane-bound protein fractions from the patient's liver sample. / Proteins (100 μg) were separated in the first dimension by IEF using carrier ampholytes pH 3 to 10. Separation in the second dimension was performed using an acrylamide gradient (10%-16%) followed by silver staining. The relative molecular mass (Mr) axis was calibrated by standard proteins (Protein Mr Marker Kit, Pierce). (A) The 2-DE pattern of soluble protein fraction. The areas of IgA and IgG heavy chains as well as κ light chain are underlined, spot 25 (25 kDa/pI 5.6) is marked by arrow. (B) The 2-DE pattern of the membrane-bound protein fraction. The spots chosen for mass spectrometry were marked by arrows (spots: 25, 23, 22, 20, 13-1, 13-2, and 13-3). Unit for the x-axis is pI; y-axis, MW (molecular weight; kDa).$

The 2-DE of the soluble and membrane-bound protein fractions from the patient's liver sample.

Proteins (100 μg) were separated in the first dimension by IEF using carrier ampholytes pH 3 to 10. Separation in the second dimension was performed using an acrylamide gradient (10%-16%) followed by silver staining. The relative molecular mass (M_r) axis was calibrated by standard proteins (Protein M_r Marker Kit, Pierce). (A) The 2-DE pattern of soluble protein fraction. The areas of IgA and IgG heavy chains as well as κ light chain are underlined, spot 25 (25 kDa/pI 5.6) is marked by arrow. (B) The 2-DE pattern of the membrane-bound protein fraction. The spots chosen for mass spectrometry were marked by arrows (spots: 25, 23, 22, 20, 13-1, 13-2, and 13-3). Unit for the x-axis is pI; y-axis, MW (molecular weight; kDa).

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