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Fine‐Specificity of the λ and χ L Chains Associated with Antibodies Directed to α(l→3) Glucosyls in Dextran
Author(s) -
BELL C.G.
Publication year - 1983
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.1365-3083.1983.tb00881.x
Subject(s) - microbiology and biotechnology , antibody , chemistry , epitope , dextran , biology , biochemistry , immunology
The function of BALB/c primary B precursors, responding to dextran (dex) B‐1355. and the fine‐specificity of the B‐1355‐binding. λ and χ, monufocal antibody (Ab) generated by the precursors have been examined. In splenic fragments from Lymulus polyphemus haemocyanin (LPH)‐primed, lethally irradiated, euthymic or nu/nu BALB/c mice cultured with thymus‐independent (TI)dex B‐1355, B‐1355‐lipopulysaccharide (LPS). B‐1355‐LPS‐LPH. or thymus‐dependent (TD) dex B‐1355‐LPH, the λ 1 precursors responded with B‐1355‐binding Ab substantially equally with respect to precursor frequency, rate of Ah production, and range of fine‐specificity, hut not with respect to frequency of the IdX and IdI isotypes related to the V H and D H associated with the λ 1 . The λ 2 contributed minimally to the repertoire. The χ precursors responded with B‐1355‐binding Ab at a rate nearly equal to the λ 1 only under TD stimulus in cuthymic fragments. A comparison of the λ 1 and χ Ah fine‐specificity, by inhibition of binding with dex differing in epitope contents and configurations, showed marked restriction in the χ relative to the λ 1 . Only approximately 10% of the relatively more abundant χ TD response showed fine α(1→3) specificity similar to that of the λ 1 . The λ 1 fine‐specificity diversity resided mainly in the IdI fraction.