Human somatotropin: Semisynthesis of the hormone by noncovalent interaction of the NH 2-terminal fragment with synthetic analogs of the COOH-terminal fragment

Abstract

Complementation of the natural NH 2-terminal fragment (consisting of 134 amino acid residues) with synthetic analogs of COOH-terminal fragments of 52 or 47 amino acids of reduced-carbamidomethylated human somatotropin gave recombinants with full growth-promoting activity as evidenced by the tibia test. Radioimmunoassay data show that the semisynthetic recombinant hormones possess nearly full immunoreactivity as compared to the native molecule.