Bovine growth hormone fragment (1–133) has in-vitro somatomedin-like activity

in Journal of Endocrinology
Authors:
J. P. Liberti
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L. A. Durham III
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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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