Christensen P, Johansson B G, Kronvall G
Acta Pathol Microbiol Scand C. 1976 Apr;84(2):73-6. doi: 10.1111/j.1699-0463.1976.tb00001.x.
The capacity of human IgG to interact with beta-haemolytic streptococci was studied in order to localize the site of interaction on the IgG molecule. The reactivity of different proteolytic fragments of IgG with streptococci group A, type M 1 and type M 56, group C and group G, was investigated by measuring their inhibitory effect on the uptake of 125I labelled IgG myeloma protein by the streptococci. Equivalent molar amounts of Fc fragment and undigested IgG inhibited the uptake of 125I labelled IgG myeloma protein equally well while only slight inhibition was obtained by F(ab')2 preparations. No reactivity was found with IgM, Fab or chymotrypsin produced fragment Fc', of IgG. The reactivity of IgG with the streptococci was localized to the Fc fragment. Since the Fc' fragment was non-reactive, the CH2 domain was probably carrying the IgG structures involved in the interaction with streptococci.
为了确定人IgG与β-溶血性链球菌相互作用的位点，对人IgG与β-溶血性链球菌相互作用的能力进行了研究。通过测量不同蛋白水解片段对链球菌摄取125I标记的IgG骨髓瘤蛋白的抑制作用，研究了IgG不同蛋白水解片段与A组、M1型和M56型、C组和G组链球菌的反应性。等摩尔量的Fc片段和未消化的IgG对125I标记的IgG骨髓瘤蛋白摄取的抑制作用相同，而F(ab')2制剂仅产生轻微抑制作用。未发现IgM、Fab或IgG的胰凝乳蛋白酶产生的片段Fc'有反应性。IgG与链球菌的反应性定位于Fc片段。由于Fc'片段无反应性，CH2结构域可能携带参与与链球菌相互作用的IgG结构。
