Open AccessHuman pituitary growth hormone: a biologically active hendekakaihekaton peptide fragment corresponding to amino-acid residues 15-125 in the hormone molecule.
Author(s) -
Choh Hao Li
Publication year - 1975
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.72.10.3878
Subject(s) - cyanogen bromide , chemistry , circular dichroism , biochemistry , peptide , amino acid , residue (chemistry) , peptide sequence , biological activity , pituitary gland , stereochemistry , hormone , in vitro , gene
A hendekakaihekaton peptide fragment has been prepared by cyanogen bromide cleavage of the NH2-terminal 134-residue fragment of human pituitary growth hormone. It was characterized by amino-acid and end-group analyses, exclusion chromatography, disc electrophoresis, circular dichroism, and ultracentrifugation. The fragment, corresponding to amino-acid residues 15-125 in the hormone molecule, possesses hepatic ornithine decarboxylase (EC 4.1.1.17; L-ornithine carboxy-lyase) stimulating, lactogenic, and somatotrophic activity. It has immunoreactivity in the microcomplement-fixation and radioimmunoassay experiments. The circular dichroism data indicate that the hendekakaihekaton peptide fragment is devoid of secondary and tertiary structure.