TY - JOUR
T1 - Binding of human IgM from a rheumatoid factor to IgG of 12 animal species
AU - Hamako, Jiharu
AU - Ozeki, Yasuhiro
AU - Matsui, Taei
AU - Yamamoto, Yoshinobu
AU - Inoue, Takashi
AU - Yukitake, Jun
AU - Titani, Koiti
N1 - Funding Information:
Acknowledgments--This work was supported in part by Grants-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan and from the Fujita Health University. We thank Dr. Stephen Anderson for editing the manuscript.
PY - 1995/12
Y1 - 1995/12
N2 - The binding of IgM from a rheumatoid factor (RF-IgM) to IgG from 12 animal species was analyzed by an ELISA system. The RF-IgM bound various animal IgG with dissimilar affinities. The binding of RF-IgM to animal IgG was inhibited by addition of protein A, which binds some animal IgG by recognizing the junctional site on CH2-CH3 domains in the Fc region. As previously reported, no significant correlation was observed between the binding of RF-IgM to IgG and the content of galactose-free oligosaccharides, which is increased in IgG of rheumatoid arthritis patients or autoimmune mice. We suggest that the crucial epitope of IgG for RF-IgM binding is not the oligosaccharide structure generated specifically in IgG of autoimmune diseases but that RF-IgM may recognize a certain protein conformation of a region in IgG near the binding site of protein A.
AB - The binding of IgM from a rheumatoid factor (RF-IgM) to IgG from 12 animal species was analyzed by an ELISA system. The RF-IgM bound various animal IgG with dissimilar affinities. The binding of RF-IgM to animal IgG was inhibited by addition of protein A, which binds some animal IgG by recognizing the junctional site on CH2-CH3 domains in the Fc region. As previously reported, no significant correlation was observed between the binding of RF-IgM to IgG and the content of galactose-free oligosaccharides, which is increased in IgG of rheumatoid arthritis patients or autoimmune mice. We suggest that the crucial epitope of IgG for RF-IgM binding is not the oligosaccharide structure generated specifically in IgG of autoimmune diseases but that RF-IgM may recognize a certain protein conformation of a region in IgG near the binding site of protein A.
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U2 - 10.1016/0305-0491(95)00121-2
DO - 10.1016/0305-0491(95)00121-2
M3 - Article
C2 - 8590381
AN - SCOPUS:0029585282
SN - 0305-0491
VL - 112
SP - 683
EP - 688
JO - Comparative Biochemistry and Physiology -- Part B: Biochemistry and
JF - Comparative Biochemistry and Physiology -- Part B: Biochemistry and
IS - 4
ER -