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.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002942:Circular Dichroism; D005260:Female; D013006:Growth Hormone / Q000378:metabolism; D006801:Humans; D008099:Liver / Q000378:metabolism; D008321:Mammary Glands, Animal / Q000378:metabolism; D010446:Peptide Fragments; D011247:Pregnancy; D011487:Protein Conformation; D011817:Rabbits; D011956:Receptors, Cell Surface / Q000378:metabolism; D011986:Receptors, Somatotropin; D012756:Sheep; D013045:Species Specificity; D013917:Thrombin / Q000378:metabolism*
D000596:Amino Acids; D010446:Peptide Fragments; D011956:Receptors, Cell Surface; D011986:Receptors, Somatotropin; D013006:Growth Hormone; D013917:Thrombin