The human teratoma cell line Tera 2 synthesizes and secretes insulin like growth factors into the culture medium. Size fractionation of conditioned medium by acidic gel filtration chromatography showed that the medium contains the canonical 7 kD IGF II, as well as a large IGF II variant, immunologically crossreactive with canonical IGF II. Amino acid analysis of the Tera 2 secreted large IGF II variant has shown that it is biochemically distinct from previously isolated high molecular weight variants of IGF II. Both species of IGF II support cell multiplication of Tera 2 cultures, albeit with different potency. In spite of the resulting potential for autocrine growth of Tera 2, we failed to observe such a situation. We propose that one reason for this failure to observe such a situation. We propose that one reason for this failure is the co-secretion of the 29 kD IGF binding protein type 1 with IGF II, which we have demonstrated to inhibit the biological effects of the growth factor on Tera 2 cells.