2012 Volume 59 Issue 1 Pages 73-79
Previously we reported neutralization and partial purification of TSAb and TBAb activity using heterophilic antibody (Ab) to animal IgG from Graves’ disease. Thus, we examined immunological similarity of TSAb and TBAb with animal IgG using experimentally generated anti-animal IgG [dog (d), bovine (b), porcine (p) and rabbit (rb)] Abs. TBII activity of TSAb- and TBAb-positive serum was neutralized by these anti-animal IgG Abs. Applied TSAb- or TBAb-IgG protein (purified by Protein A) on these anti-animal IgG Abs-bound column was found mainly in the unbound fraction (UF)(>65%) and partially in the bound fraction(BF)(<35%). The TBII and TSAb activity of TSAb-IgG in the BF showed significantly higher than the UF. Thus, the ratio of TBII activity (U/L)/mg protein in the BF/UF was high. TBII activity of TBAb-IgG was similarly purified by this column. We examined immunological characteristics of TSAb-and TBAb-Fab or F(ab’)2 using rabbit anti-bF(ab’)2 Ab. TBII and TSAb activity of TSAb-Fab or- F(ab’)2 and TBII activity of TBAb-Fab or -F(ab’)2 were neutralized by anti-bF(ab’)2 Ab. Partial purification of TSAb- or TBAb-Fab and -F(ab’)2 by anti-bF(ab’)2 Ab-bound column was also possible. Immunological similarity of TSAb- and TBAb-IgG with animal IgG such as d, b, p, rb by anti-animal IgG Ab, and TSAb- or TBAb-Fab and -F(ab’)2 with bFab by anti-bF(ab’)2 Ab were demonstrated. These fact suggest that both Fab and Fc portion of TSAb- and TBAb-IgG molecule have immunological similarity with animal IgG.
