Igg-Dependent Hydrolysis of Myelin Basic Protein of Patients with Different Courses of Schizophrenia

Figure 4

(a) Graph of MBP-hydrolyzing activity of extracts from various gel fragments after SDS-PAGE of an IgG preparation. (b) Electrophoretic analysis of IgG protein. Assay of MBP-hydrolyzing activity of purified IgG after SDS-PAGE in 4–15% gradient gel; the gel was incubated under special conditions for renaturation of the Abs. The relative proteolytic activity (RA. %) was revealed using extracts of many 2–3 mm fragments of one longitudinal slice of the gel. The RA of IgG corresponding to complete hydrolysis of 0.5 mg/mL MBP after incubation for 24 h with 10 μl of the extract was taken for 100%. The average error in the initial rate determination from three experiments did not exceed 10–15%. The second set of control longitudinal slices of the same gels corresponding to IgGs before (lane 1) and after (lane 3) incubation with DTT was stained with silver. Lane 2 shows the position of molecular mass markers. The IgG—band is in the region of 150 kDa, which corresponds to the native IgG; the H—band is in the region of 50 kDa, which corresponds to the heavy chains of IgG after incubation with DTT; the L—band in the region of 25 kDa, which corresponds to the light chains of IgG after incubation with DTT.

(a)

(b)