H-2D antigens released by thymocytes and cell adhesion.

The identity and complete purification of mouse Thymocyte Interaction Modulation Factor (T IMF) is described. Use of silver-stained PAGE methods shows that previous methods of purification yield preparations containing two protein or glycoprotein bands. T IMF activity from H-2k mice can be bound to 15.5.5 monoclonal antibody columns (anti H-2 Dk) but not to 11.4.1 columns (anti H-2 Kk). The activity can be recovered from 15.5.5 columns and runs on PAGE aa a single band at approximately 34,000 Daltons. This evidence together with previous evidence relating the activity to H-2D locus argues that T IMF is a soluble H-2 D antigen fragment equivalent to a papainized H-2 fragment. Additional evidence is presented on an improved method of assay of T IMF activity, on its inactivation by enzymes and serine-esterase inhibitors and of its effect on syngeneic leucocytes and macrophages. It is shown that T IMF is not appreciably toxic cells.