MOLECULAR PROPERTIES OF T‐LYMPHOMA IMMUNOGLOBULIN: II. PEPTIDE COMPOSITION OF THE HEAVY CHAIN

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Abstract
In order to obtain structural information and to facilitate studies of the covalent structure of T-cell immunoglobulin, we have performed investigations of the peptide fragments of the heavy chain of this molecule, on a comparative basis, with heavy chains of serum immunoglobulins. T-cell immunoglobulin was isolated from 125I-labelled culture medium of monoclonal continuously cultured T-lymphoma cells by means of immunoadsorbents. Peptides were prepared from the purified 125I-labelled heavy chain by means of cleavage with cyanogen bromide or digestion with trypsin. We then resolved these peptides and compared them with those peptides derived from 131I-labelled murine mu, gamma and alpha chains separately and in mixed label experiments by means of polyacrylamide gel electrophoresis in sodium dodecyl sulfate containing buffers, 2 dimensional peptide mapping and ion exchange chromatography. The profiles of the radiolabelled peptides obtained from the T-lymphoma heavy chains were quite distinct from those of murine gamma chains but indicated a structural similarity to both mu and alpha chains, which share some common peptides. These results are consistent with the antigenic and physicochemical data available and suggest that T-cell immunoglobulin is a new isotype that shows similarities to IgA and IgM, but of which the precise nature of the constant region has yet to be delineated.