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. 2012 Mar 28;287(21):17765–17776. doi: 10.1074/jbc.M111.314468

FIGURE 1.

FIGURE 1.

Characterization of the 36-kDa protein detected by the serum IgG of a patient with CIDP. A, Western blotting of rat brain and ScN whole homogenates (10 μg protein). The 36-kDa band was detected in the ScN but not in the brain homogenate. B and C, Western blotting of the ScN fractions using the patient serum (Pt). The 36-kDa protein was detected in the membrane fraction (Mem) but not in the cytosolic fraction (Cyt; B) and was enriched in the myelin fraction (Myln; C). While β-actin and GAPDH (cytosolic and membrane-associated proteins) were detected both cytosolic and membrane fractions, β-catenin (adherence junction marker) was extremely enriched in the membrane fraction (B). In the myelin fraction, MBP molecules (myelin marker) were enriched but not β-catenin, GAPDH, nor paxillin (focal contact marker) (C). D, after deglycosylation of N-linked sugar chains with PNGase F treatment of ScN whole homogenate, the relative molecular weight of the 36-kDa protein was shifted down in the same manner as P0. WH, whole homogenates; Nrml, negative control using normal human serum; M, marker.