Biochemical characteristics of the IJ molecule

The actual I-J structure has not been identified with any certainty. However, the suppressor factors which are recognized by polyclonal and monoclonal I-J-specific antibodies are protein in nature. The I-J-bearing polypeptide may be found either alone or linked (by a disulfide bridge) to a second (non-I-J-bearing) polypeptide. The two-chain factors are usually composed of an I-J-bearing chain linked to an antigen-binding chain. The I-J-bearing chain appears in most cases to be a polypeptide of 25-30 kDa. The antigen-binding chain may represent some part of the T cell receptor a chain.

The I-J structure expressed on the surface of both helper and suppressor T cells has also been examined. Using NP-40 lysates and immunoprecipitation with I-J-specific antibodies, the I-J molecule is detected as an 81-90 kDa dimer composed of 42-46 kDa glycoprotein subunits. In these studies, the I-J dimer was found to be distinct from the T cell receptor a/fi heterodimer.

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