Bovine growth hormone fragment (1–133) has in-vitro somatomedin-like activity
- 1 February 1983
- journal article
- research article
- Published by Bioscientifica in Journal of Endocrinology
- Vol. 96 (2) , 195-199
- https://doi.org/10.1677/joe.0.0960195
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.This publication has 2 references indexed in Scilit:
- The generation of sulfation factor activity by proteolytic modification of growth hormone.Journal of Biological Chemistry, 1980
- Fragments of Human Growth Hormone Produced by Digestion with Thrombin: Chemistry and Biological Properties*Endocrinology, 1980