Abstract
Thrombin digestion of bovine growth hormone (1-191) resulted in cleavage of the peptide bond between amino acid residues 133 and 134. Native growth hormone and purified peptides (1-133) and (134-191) were assayed for somatomedin-like activity. Peptide (1-133), ranging in concentration from 0.15-15 nmol/l, stimulated in-vitro uptake of [3H]thymidine by rat costal cartilage. None of the other peptides was biologically active.
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