Human somatotropin: biological characterization of the recombinant molecule.
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.
D000595:Amino Acid Sequence; D000818:Animals; D001681:Biological Assay; D004790:Enzyme Induction / Q000187:drug effects; D000939:Epitopes; D005341:Fibrinolysin; D013006:Growth Hormone / Q000276:immunology / Q000494:pharmacology; D006801:Humans; D008321:Mammary Glands, Animal / Q000378:metabolism; D009955:Ornithine Decarboxylase / Q000096:biosynthesis; D014176:Protein Biosynthesis; D013329:Structure-Activity Relationship
D000939:Epitopes; D013006:Growth Hormone; D005341:Fibrinolysin; D009955:Ornithine Decarboxylase