Masuho Y, Tomibe K, Matsuzawa K, Ohtsu A
Vox Sang. 1977;32(3):175-81. doi: 10.1111/j.1423-0410.1977.tb00622.x.
S-sulfonated gamma-globulin (S-GG) was prepared by treating gamma-globulin with sulfite and tetrathionate ions. About four 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. Furthermore, S-GG was found to maintain satisfactory levels for prolonged periods in vivo. The physicochemical and antigenic analyses of S-GG suggest that the S-sulfonation induces structural modification only at restricted sites.
通过用亚硫酸根离子和连四硫酸根离子处理γ-球蛋白制备了S-磺化γ-球蛋白(S-GG)。约四个链间二硫键被选择性裂解,生成S-磺酸根基团。尽管上述处理强烈抑制了抗补体活性和非特异性皮肤反应性,但所得的S-GG仍保留高抗体活性。此外,发现S-GG在体内能长时间维持令人满意的水平。对S-GG的物理化学和抗原分析表明,S-磺化仅在有限的位点诱导结构修饰。