Human somatotropin: biological characterization of the recombinant molecule

Li, C. H. ; Hayashida, T. ; Doneen, B. A. ; Rao, A. J. (1976) Human somatotropin: biological characterization of the recombinant molecule PNAS, 73 (10). pp. 3463-3465. ISSN 0027-8424

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Official URL: http://www.pnas.org/content/73/10/3463.short

Abstract

The recombinant hormone obtained by non-covalent interaction of the NH2-terminal 134 amino acid fragment with the COOH-terminal 51 amino acid fragment of the reduced-carbamidomethylated human somatotropin molecule is found to exhibit nearly full biological activity of the native hormone, as evidenced by the stimulation of hepatic ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) in vivo and protein synthesis in mouse mammary gland in vitro. Radioimmunoassay data indicate that the recombinant behaves immunochemically in a manner almost identical to that of the native hormone.

Item Type:Article
Source:Copyright of this article belongs to National Academy of Sciences.
ID Code:42992
Deposited On:08 Jun 2011 13:32
Last Modified:18 May 2016 00:06

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