Abstract
The structures recognized by monoclonal anti-IgG1 rheumatoid factors (RF) were localized by testing their reactivity with mutant immunoglobulins carrying γ1 chains that lacked either the C(H)1 or the C(H)3 domains. While optimal binding was observed in the absence of C(H)1, deletion of C(H)3 completely abolished the reactivity of all but one of the 71 monoclonal RF tested. Similar experiments were carried out with IgG2a- and IgG2b-specific RF by using variant immunoglobulins carrying various hybrid γ2a-γ2b heavy chains. It was found that both the polyclonal RF produced by autoimmune strains, MRL/MpJ-1pr and NZB/BinJ, and most of the monoclonal RF derived from normal strains, BALB/c, C57Bl/6, and 129/Sv, were directed against determinants located in a segment spanning the C-terminal 8 residues of the C(H)2 domain and the complete C(H)3 domain.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1763-1768 |
| Number of pages | 6 |
| Journal | Journal of Experimental Medicine |
| Volume | 158 |
| Issue number | 5 |
| State | Published - 1983 |
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ASJC Scopus subject areas
- Immunology
Cite this
Determinants recognized by murine rheumatoid factors : Molecular localization using a panel of mouse myeloma variant immunoglobulins. / Stassin, V.; Coulie, P. G.; Birshtein, B. K.; Secher, D. S.; Van Snick, J.
In: Journal of Experimental Medicine, Vol. 158, No. 5, 1983, p. 1763-1768.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Determinants recognized by murine rheumatoid factors
T2 - Molecular localization using a panel of mouse myeloma variant immunoglobulins
AU - Stassin, V.
AU - Coulie, P. G.
AU - Birshtein, B. K.
AU - Secher, D. S.
AU - Van Snick, J.
PY - 1983
Y1 - 1983
N2 - The structures recognized by monoclonal anti-IgG1 rheumatoid factors (RF) were localized by testing their reactivity with mutant immunoglobulins carrying γ1 chains that lacked either the C(H)1 or the C(H)3 domains. While optimal binding was observed in the absence of C(H)1, deletion of C(H)3 completely abolished the reactivity of all but one of the 71 monoclonal RF tested. Similar experiments were carried out with IgG2a- and IgG2b-specific RF by using variant immunoglobulins carrying various hybrid γ2a-γ2b heavy chains. It was found that both the polyclonal RF produced by autoimmune strains, MRL/MpJ-1pr and NZB/BinJ, and most of the monoclonal RF derived from normal strains, BALB/c, C57Bl/6, and 129/Sv, were directed against determinants located in a segment spanning the C-terminal 8 residues of the C(H)2 domain and the complete C(H)3 domain.
AB - The structures recognized by monoclonal anti-IgG1 rheumatoid factors (RF) were localized by testing their reactivity with mutant immunoglobulins carrying γ1 chains that lacked either the C(H)1 or the C(H)3 domains. While optimal binding was observed in the absence of C(H)1, deletion of C(H)3 completely abolished the reactivity of all but one of the 71 monoclonal RF tested. Similar experiments were carried out with IgG2a- and IgG2b-specific RF by using variant immunoglobulins carrying various hybrid γ2a-γ2b heavy chains. It was found that both the polyclonal RF produced by autoimmune strains, MRL/MpJ-1pr and NZB/BinJ, and most of the monoclonal RF derived from normal strains, BALB/c, C57Bl/6, and 129/Sv, were directed against determinants located in a segment spanning the C-terminal 8 residues of the C(H)2 domain and the complete C(H)3 domain.
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M3 - Article
C2 - 6195294
AN - SCOPUS:0021046421
VL - 158
SP - 1763
EP - 1768
JO - Journal of Experimental Medicine
JF - Journal of Experimental Medicine
SN - 0022-1007
IS - 5
ER -