Development of an Intravenous γ‐Globulin with Fc Activities

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Abstract
S-sulfonated .gamma.-globulin (S-GG) was prepared by treating .gamma.-globulin with sulfite and tetrathionate ions. About 4 interchain disulfide bonds were selectively cleaved to give S-sulfonate groups. Although the above treatment strongly suppresses anticomplementary activity and nonspecific skin reactivity, the resulting S-GG retains high antibody activity. S-GG maintained satisfactory levels for prolonged periods in vivo. The physiocochemical and antigenic analyses of S-GG suggest that the S-sulfonation induces structural modification only at restricted sites.