Premium
Binding Affinity of Human Autoantibodies: Studies of Cryoglobulin IgM Rheumatoid Factors and IgG Autoantibodies to Albumin
Author(s) -
WAGER O.,
TEPPO A.M.
Publication year - 1978
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1978.tb00484.x
Subject(s) - autoantibody , cryoglobulin , autoimmunity , immunology , rheumatoid factor , antibody , human serum albumin , chemistry , affinities , medicine , biochemistry , cryoglobulinemia , hepatitis c virus , virus
The binding affinity of cryoglobulin IgM rheumatoid factors (RF) for human IgG and of human IgG anti‐albumin autoantibodies for HSA was measured by the molecular sieving technique. The binding affinities of the two autoantibodies were consistently low (10 4 ‐10 5 I/M) as compared to the affinities of corresponding hyperimmune animal antibodies (10 6 ‐10 8 I/M). The findings were discussed in relation to theories on human autoimmunity. The existence of strict autotolerance at the T cell level and of autoreactivity at the low affinity B cell level was considered to be best compatible with the findings of this study and with the major known facts of autoimmunity.