Hunneyball I M, Stanworth D R
Immunology. 1976 Apr;30(4):579-86.
Human IgG1 Fc fragment was digested at neutral pH by thermolysin, producing two large subfragments: one comprising the major part of the Fc fragment but devoid of the hinge region; the other comprising the Cgamma3 domain. The former fragment retained the capacity to react with "general" rheumatoid factors whereas the latter did not, indicating that the binding site for "general" rheumatoid factors on the Fc fragment of human IgG1 does not involve the hinge region of the molecule.
人IgG1 Fc片段在中性pH条件下被嗜热菌蛋白酶消化，产生两个大片段：一个包含Fc片段的主要部分，但没有铰链区；另一个包含Cγ3结构域。前一个片段保留了与“普通”类风湿因子反应的能力，而后一个片段则没有，这表明人IgG1 Fc片段上“普通”类风湿因子的结合位点不涉及分子的铰链区。
