Bouvet J P, Pires R, Quan C, Iscaki S, Pillot J
Unité d'Immunologie Microbienne, WHO Center of Reference and Research on Viral Hepatitis, Institut Pasteur, Paris, France.
Scand J Immunol. 1991 Apr;33(4):381-6. doi: 10.1111/j.1365-3083.1991.tb01785.x.
The specificity of human F(ab)-binding Protein Fv (previously called Protein F), a sialoprotein released into the digestive tract mainly during hepatitis, was investigated with fragments or chains of monoclonal immunoglobulins. Protein Fv bound an unreduced H-chain dimer of a monoclonal human IgA2m(1) molecule but neither the corresponding L-chain dimer, nor several Bence-Jones molecules. Using enzymatic subfragments of F(ab)mu, or F(ab')2 gamma, a significant binding was observed with Fv fragments (VH + VL), while Fb fragments (CH1 + CL) were inactive. Taken altogether, these results prove that the structure recognized by Protein Fv is located in the VH domain. This structure probably involves discontinuous epitopes linked by a disulphide bond, which are destroyed by combined reduction and dissociation. Protein Fv does not interfere with the antigen-binding site, since there was no reciprocal inhibition with the antigen-antibody reaction.
人类F(ab)结合蛋白Fv（以前称为蛋白F）是一种主要在肝炎期间释放到消化道的唾液蛋白，研究人员用单克隆免疫球蛋白的片段或链对其特异性进行了研究。蛋白Fv结合单克隆人IgA2m(1)分子的未还原重链二聚体，但不结合相应的轻链二聚体，也不结合几种本-周蛋白分子。使用F(ab)μ或F(ab')2γ的酶切亚片段，观察到与Fv片段（VH + VL）有显著结合，而Fb片段（CH1 + CL）无活性。综上所述，这些结果证明蛋白Fv识别的结构位于VH结构域。该结构可能涉及由二硫键连接的不连续表位，这些表位在还原和解离的联合作用下被破坏。蛋白Fv不干扰抗原结合位点，因为抗原-抗体反应不存在相互抑制。
