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A Murine Monoclonal Multireactive Immunoglobulin Kappa Light Chain
Author(s) -
MAHANA W.,
JACQUEMART F.,
ERMONVAL M.
Publication year - 1994
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.1365-3083.1994.tb03347.x
Subject(s) - microbiology and biotechnology , immunoglobulin light chain , monoclonal antibody , antibody , chemistry , immunoassay , immunoglobulin g , spleen , polyacrylamide gel electrophoresis , dissociation constant , monoclonal , antigen , biology , gel electrophoresis , biochemistry , enzyme , receptor , immunology
N12.12 is a monoclonal immunoglobulin (Ig) kappa light chain (KLC) secreted by a B‐celI hybridoma derived from spleen cells of a normal SJA mouse. No heavy chain was detected in the culture supernatant of this hybridoma using an enzyme immunoassay (EIA) and after polyacrylamide gel eleclrophoresis (SDS‐PAGE) of the 35 S‐methionin biosynthetically labelled proteins secreted by the cells. It was shown that NI2. I2 KLC reacted with mouse actin, trinitrophenylated bovine serum album in (TNP 25 ‐BSA) and weakly with bovine myoglobin. The binding of the NI2.12 ‘monoclonal antibody’ to mouse actin or to TNP 25 ‐BSA was inhibited specifically by both antigens with a dissociation constant (K D ) for binding to mouse actin of 10 −7 M. The results indicate that a free KLC can bind both to mouse and to non‐mouse molecules, thus exhibiting binding characteristics usually attributed to natural multireaetive antibodies.