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Journal of Endocrinology (1983) 96, 195-199       DOI: 10.1677/joe.0.0960195
© 1983 Society for Endocrinology
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Bovine growth hormone fragment (1–133) has in-vitro somatomedin-like activity

J. P. Liberti and L. A. Durham, III

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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