This communication reports the action of bovine thrombin on, ovine, bovine and human growth hormones. Thrombin cleavage was shown to be restricted to a single homologous peptide bond in all three growth hormones (at sequence positions 133–134 of the ovine and bovine hormones). Ovine growth hormone was the most sensitive, to the action of thrombin, bovine growth hormone was attacked to a relatively less extent, and human growth hormone was the most resistant to the enzyme. After reduction and carbamidomethylation of the disulfide bonds in thrombin modified ovine growth hormone, the two fragments (residues 1–133 and 134–191) were isolated. The large N H2‐terminal thrombin fragment of the hormone (residues 1 – 133) was found to be inactive in the rat tibia test, whereas a tryptic fragment (residues 96‐133) isolated in an independent way gave measurable responses.
|Number of pages||8|
|Journal||European Journal of Biochemistry|
|Publication status||Published - May 1976|
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