Insulin-like growth factors I and II of nonmammalian sera.

We have compared the insulin-like growth factors (IGFs) of a number of mammalian and nonmammalian vertebrate sera. Sera were subjected to acid gel filtration through G-75 Sephadex and separate binding protein and free IGF fractions were pooled. The IGF pools were subjected to flatbed isoelectric focusing and the concentration of IGF I in the fractions was detected with an immunoassay using 125I-hIGF I and the somatomedin C antibody of Underwood and Van Wyk. IGF II in the fractions was detected with either the 125I-IGF rat placental membrane RRA or the 125I-IGF II serum binding protein assay. One or more basic peaks of IGF I immunoactivity were detected in all the mammalian sera studied (human, guinea pig, rat, bovine, kangaroo, and opossum) and all the nonmammalian species studied (chicken, turtle, toad, and trout). Neutral and slightly acidic peaks of IGF II receptor reactivity were observed in human, cow, and guinea pig serum. No distinct peaks of IGF II were observed in adult rat, opossum, or kangaroo serum. Distinct peaks of IGF II activity in the neutral to slightly acidic range were clearly recognized in chicken and turtle serum, no such peaks were recognized in toad and trout serum. All mammalian sera studied contained acid stable, binding proteins with high affinity, saturable binding of 125I-IGF II. None of the nonmammalian sera studied contained demonstrable specific 125I-IGF II binding. These observations document the presence of separate IGF I and IGF II peptides in chickens and turtles but only IGF I in amphibians and fish. These observations indicate that the gene duplication giving rise to two separate IGFs arose before reptilian evolution. The acquisition of a specific IGF binding protein is limited to mammals.