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MOLECULAR PROPERTIES OF T‐LYMPHOMA IMMUNOGLOBULIN
Author(s) -
Moseley Jane M.,
Beatty Elizabeth A.,
Marchalonis J. J.
Publication year - 1979
Publication title -
international journal of immunogenetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.41
H-Index - 47
eISSN - 1744-313X
pISSN - 1744-3121
DOI - 10.1111/j.1744-313x.1979.tb00672.x
Subject(s) - immunoglobulin light chain , microbiology and biotechnology , antibody , surface immunoglobulin , sodium dodecyl sulfate , cyanogen bromide , gel electrophoresis , chemistry , trypsin , antigen , biology , biochemistry , b cell , gene , enzyme , peptide sequence , immunology
SUMMARY Structural studies of T‐cell immunoglobulin light chains have been carried out in order to ascertain whether they possess a unique structure or if they resemble standard kappa or lambda isotypes. T‐cell immunoglobulin was isolated from 125 I‐labelled culture medium of monoclonal, continuously cultured T‐lymphoma cells, and the purified 125 I‐labelled light chains were subjected to either cleavage by cyanogen bromide or digestion with trypsin. These peptides were then resolved and compared with those derived from 125 I‐ and 131 I‐labelled murine kappa and lambda chains in mixed label experiments, by means of polyacrylamide gel electrophoresis in sodium dodecyl sulfate‐containing buffers and ion exchange chromatography. The profiles obtained suggested that T‐lymphoma immunoglobulin light chains are immunoglobulin polypeptides and most closely resemble kappa chains. These results support available antigenic and mRNA hybridization data, which also suggest that T cells bear kappa‐like light chains.