Two contiguous thrombin fragments of human somatotropin form a functionally active recombinant, but the two homologous fragments from sheep hormone do not.

Two thrombin fragments of reduced-carbamidomethylated human somatotropin representing the full primary structure of the native hormone (residues 1-134 and 135-191) have been found to form a recombinant molecule with properties similar to those of reduced-carbamidomethylated human somatotropin as shown by circular dichroism spectroscopy, two receptor-binding assays, and radioimmunoassay. In contrast, the homologous thrombin fragments of reduced-carbamidomethylated sheep hormone (residues 1-133 and 134-191) do not undergo recombination. Furthermore, neither the reduced-alkylated nor the reduced and nonalkylated C-terminal thrombin fragment of sheep hormone is able to interact with the reduced-carbamidomethylated N-terminal thrombin fragment of human hormone, under conditions which favor the recombination of the two human somatotropin fragments.