Premium
Antigenic determinants in the N‐terminal halves of human κ‐chains; their relation to the variable region subgroups
Author(s) -
Orlans Eva,
Pearce Cheryl A.
Publication year - 1974
Publication title -
european journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.272
H-Index - 201
eISSN - 1521-4141
pISSN - 0014-2980
DOI - 10.1002/eji.1830040206
Subject(s) - antiserum , polyclonal antibodies , bence jones protein , immunoglobulin light chain , biology , population , monoclonal antibody , antigen , antibody , epitope , microbiology and biotechnology , genetics , demography , sociology
Abstract Antibodies directed against the variable (V) regions of both the heavy and light chains are found consistently in fowl antisera to polyclonal human F(ab′) 2 . When tested by absorption and precipitation with κ‐Bence‐Jones proteins of known amino acid sequences, nearly all such antisera were found to contain antibodies specific for one or more of the three basic V κ sequences. This result indicates that a very high proportion of the normal κ‐chain population carries determinants which correspond to sequence patterns derived from analyses of pathological monoclonal proteins. Although it was possible to determine the V κ subgroups of some intact monoclonal immunoglobulins with antisera, the procedure has serious limitations. One of these is the need to absorb all antibody to V H ‐region antigens with suitable monoclonal λ proteins; of 14 IgM proteins examined with such absorbed antisera, 8 were found to have κI light chains, 3 were κIII, I was κII, and 2 could not be classified. Another limitation, which applies also to Bence‐Jones proteins, is the occurrence of antigenically deficient κ‐chains, accounting for 10–20% of the proteins tested. One such protein (κIII Rad) did not precipitate with most of the anti‐V κIII sera, but differed in only 7 positions from the basic κIII sequence.