Binding of human IgM from a rheumatoid factor to IgG of 12 animal species

Jiharu Hamako, Yasuhiro Ozeki, Taei Matsui, Yoshinobu Yamamoto, Takashi Inoue, Jun Yukitake, Koiti Titani

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)683-688
Number of pages6
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume112
Issue number4
DOIs
Publication statusPublished - 12-1995

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Binding of human IgM from a rheumatoid factor to IgG of 12 animal species'. Together they form a unique fingerprint.

  • Cite this