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- Title
Non-immune VH-binding Specificity of Human Protein Fv.
- Authors
Bouvet, J. P.; Pires, R.; Quan, C.; Iscaki, S.; Pillot, J.
- Abstract
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)μ, or F(ab')2γ, 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.
- Subjects
CARRIER proteins; HEPATITIS; LIVER diseases; ANTIGENS; IMMUNOGLOBULINS; PLASMA cells
- Publication
Scandinavian Journal of Immunology, 1991, Vol 33, Issue 4, p381
- ISSN
0300-9475
- Publication type
Article
- DOI
10.1111/j.1365-3083.1991.tb01785.x