Our laboratory has previously reported the isolation of a serum blocking factor (SBF) from infectious mononucleosis (IM) patients. The SBF has been purified by a combination of Sephadex QAE-50 ion exchange and Sephadex G-200 molecular sieve chromatography. This material was found to be devoid of soluble immune complexes, and immunochemically and biochemically was characterized as IgG and, hence, termed SBF-IgG. The SBF-IgG was shown to significantly (alpha = 0.05) suppress antigen specific (Influenza A-1[H1N1]) in vitro lymphocyte stimulation (LS) as well as leukocyte migration-inhibition (LMI) reactivity. Also, the SBF-IgG significantly suppressed the in vitro.LS response to phytohemagglutinin. In addition, the SBF-IgG when bound to normal donor lymphocytes significantly reduced the high affinity E-rosette (HAR) reactivity at 29 degrees C. A purified T lymphocyte subpopulation of normal donor lymphocytes specifically bound SBF-IgG, and the latter could be r covered using glycine-HCI. It appears that SBF-IgG is a nonspecific antibody; it binds neither lymphokines nor specific antigen, but apparently elicits its in vitro vitro cell-mediated suppressive effect at the level of the T lymphocytes.