期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1976
卷号：73
期号：10
页码：3463-3465
DOI：10.1073/pnas.73.10.3463
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
