Literature DB >> 8508555

IgM rheumatoid factor and the inhibition of covalent binding of C4b to IgG in immune complexes.

J N Jarvis1, J C Lockman, R P Levine.   

Abstract

Work by other investigators has shown that IgM-rheumatoid factors (IgM-RF's) can impede complement-mediated inhibition of immune precipitation. We examined the binding of complement component C4b to radiolabelled IgG in model immune complexes and demonstrate that IgM-RF's are capable of reducing the covalent binding of C4b to 125I-IgG in the complexes. Reduced binding to IgG, however, may not be accompanied by binding of C4b to IgM-RF's within the complex, as we also demonstrate that IgM-RF's are relatively poor at C4b capture compared with normal IgM.

Entities:  

Mesh:

Substances:

Year:  1993        PMID: 8508555

Source DB:  PubMed          Journal:  Clin Exp Rheumatol        ISSN: 0392-856X            Impact factor:   4.473


  2 in total

1.  Mechanism of complement-dependent haemolysis via the lectin pathway: role of the complement regulatory proteins.

Authors:  C Suankratay; C Mold; Y Zhang; T F Lint; H Gewurz
Journal:  Clin Exp Immunol       Date:  1999-09       Impact factor: 4.330

2.  Composition and biological behaviour of immune complexes isolated from synovial fluid of patients with juvenile rheumatoid arthritis (JRA).

Authors:  J N Jarvis; M M Diebold; M K Chadwell; M Iobidze; H T Moore
Journal:  Clin Exp Immunol       Date:  1995-06       Impact factor: 4.330

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.