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Bovine growth hormone fragment (1-133) has in-vitro somatomedin-like activity. J Endocrinol 1983 Feb;96(2):195-9

Date

02/01/1983

Pubmed ID

6827204

DOI

10.1677/joe.0.0960195

Scopus ID

2-s2.0-0020657586 (requires institutional sign-in at Scopus site)   7 Citations

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.

Author List

Liberti JP, Durham LA 3rd

Author

Lucian A. Durham MD, PhD Associate Professor in the Surgery department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Animals
Cattle
DNA
Growth Hormone
In Vitro Techniques
Peptide Fragments
Somatomedins