Premium
Antibody Responses to λ1 J558 and λ2 315 Light Chains
Author(s) -
BOGEN B.
Publication year - 1984
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.1365-3083.1984.tb01020.x
Subject(s) - antibody , immunoglobulin light chain , immunization , myeloma protein , antigen , biology , adept , multiple myeloma , chemistry , microbiology and biotechnology , enzyme , immunology , biochemistry
Specificity of BALB/c antibody responses to A chains of isologous myeloma proteins 315 and J558 was explored by enzyme‐linked immunosorbent assay. A‐chain binding antibodies were not detected when immunizing with assembled (H + L) myeloma proteins. However, relatively high titred IgG antibodies were elicited by free λ2 315 immunization. Antibodies were directed to ‘hidden’ determinants since binding was abrogated upon H + L assembly of chains. At least a portion of antibodies bound antigenic determinants in the variable region and cross‐reacted with λl land λ3 chains. Free λ1 1558 immunization induced low‐titred, predominantly IgM antibodies that also only reacted with ‘hidden’ determinants. These determinants were most probably located in the constant (C) region and no cross‐reaction to λ2 or λ3 was observed. An artefact of technical importance was noted: myeloma proteins exposed ‘hidden’ determinants on their A chains when coated directly to polystyrene walls. This ariefactual exposition was lost when anti C‐region antibody spacer molecules were inserted between the wall and the myeloma proteins. Antibody and T helper cell (Th) responses to free λ2 315 covaried significantly in various strains while antibody and Th responses to free λ1 1558 did not. In some strains, weak antibody responses were detected without detectable Th.