Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1975 Oct;72(10):3878–3882. doi: 10.1073/pnas.72.10.3878

Human pituitary growth hormone: a biologically active hendekakaihekaton peptide fragment corresponding to amino-acid residues 15-125 in the hormone molecule.

C H Li
PMCID: PMC433099  PMID: 812085

Abstract

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.

Full text

PDF
3878

Images in this article

3881Image
on p.3881

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bewley T. A., Brovetto-Cruz J., Li C. H. Human pituitary growth hormone. Physicochemical investigations of the native and reduced-alkylated protein. Biochemistry. 1969 Dec;8(12):4701–4708. doi: 10.1021/bi00840a007. [DOI] [PubMed] [Google Scholar]
  2. Bewley T. A., Li C. H. Circular dichroism studies on human pituitary growth hormone and ovine pituitary lactogenic hormone. Biochemistry. 1972 Feb 29;11(5):884–888. doi: 10.1021/bi00755a030. [DOI] [PubMed] [Google Scholar]
  3. Böhlen P., Stein S., Stone J., Udenfriend S. Automatic Monitoring of primary amines in preparative column effluents with fluorescamine. Anal Biochem. 1975 Aug;67(2):438–445. doi: 10.1016/0003-2697(75)90316-4. [DOI] [PubMed] [Google Scholar]
  4. Clarke W. C., Hayashida T., Li C. H. Human pituitary growth hormone: immunochemical investigations of biologically active fragments. Arch Biochem Biophys. 1974 Oct;164(2):571–574. doi: 10.1016/0003-9861(74)90068-x. [DOI] [PubMed] [Google Scholar]
  5. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  6. GREENSPAN F. S., LI C. H. Bioassay of hypophyseal growth hormone; the tibia test. Endocrinology. 1949 Nov;45(5):455-63, illust. doi: 10.1210/endo-45-5-455. [DOI] [PubMed] [Google Scholar]
  7. GROSS E., WITKOP B. Nonenzymatic cleavage of peptide bonds: the methionine residues in bovine pancreatic ribonuclease. J Biol Chem. 1962 Jun;237:1856–1860. [PubMed] [Google Scholar]
  8. Jänne J., Williams-Ashman H. G. On the purification of L-ornithine decarboxylase from rat prostate and effects of thiol compounds on the enzyme. J Biol Chem. 1971 Mar 25;246(6):1725–1732. [PubMed] [Google Scholar]
  9. LI C. H., LIU W. K., DIXON J. S. Human pituitary growth hormone. VI. Modified procedure of isolation and NH2-terminal amino acid sequence. Arch Biochem Biophys. 1962 Sep;Suppl 1:327–332. [PubMed] [Google Scholar]
  10. LI C. H. Preliminary investigations on the action of pepsin on human pituitary growth hormone. J Gen Physiol. 1962 Mar;45(4):169–175. doi: 10.1085/jgp.45.4.169. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. LI C. H. Properties of and structural investigations on growth hormones isolated from bovine, monkey and human pituitary glands. Fed Proc. 1957 Sep;16(3):775–783. [PubMed] [Google Scholar]
  12. Li C. H., Dixon J. S., Lo T. B., Schmidt K. D., Pankov Y. A. Studies on pituitary lactogenic hormone. XXX. The primary structure of the sheep hormone. Arch Biochem Biophys. 1970 Dec;141(2):705–737. doi: 10.1016/0003-9861(70)90191-8. [DOI] [PubMed] [Google Scholar]
  13. Li C. H., Gráf L. Human pituitary growth hormone: isolation and properties of two biologically active fragments from plasmin digests. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1197–1201. doi: 10.1073/pnas.71.4.1197. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Li C. H., Samuelsson G. Human pituitary growth hormone. XI. Rate of hydrolysis by trypsin, chymotrypsin, and pepsin; effect of trypsin on the biological activity. Mol Pharmacol. 1965 Jul;1(1):47–52. [PubMed] [Google Scholar]
  15. Nicoll C. S. Bio-assay of prolactin. Analysis of the pigeon crop-sac response to local prolactin injection by an objective and quantitative method. Endocrinology. 1967 Apr;80(4):641–655. doi: 10.1210/endo-80-4-641. [DOI] [PubMed] [Google Scholar]
  16. Nutting D. F., Kostyo J. L., Mills J. B., Wilhelmi A. E. Dissociation of some of the biological activities of porcine and human growth hormones by cyanogen bromide cleavage. Endocrinology. 1972 May;90(5):1202–1213. doi: 10.1210/endo-90-5-1202. [DOI] [PubMed] [Google Scholar]
  17. OUCHTERLONY O. Antigen-antibody reactions in gels. IV. Types of reactions in coordinated systems of diffusion. Acta Pathol Microbiol Scand. 1953;32(2):230–240. [PubMed] [Google Scholar]
  18. Reagan C. R., Mills J. B., Kostyo J. L., Wilhelmi A. E. Biological properties of plasmin digests of S-carbamidomethylated human growth hormone. Proc Natl Acad Sci U S A. 1975 May;72(5):1684–1686. doi: 10.1073/pnas.72.5.1684. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Reagan C. R., Mills J. B., Kostyo J. L., Wilhelmi A. E. Isolation and biological characterization of fragments of human growth hormone produced by digestion with plasmin. Endocrinology. 1975 Mar;96(3):625–636. doi: 10.1210/endo-96-3-625. [DOI] [PubMed] [Google Scholar]
  20. Schalch D. S., Reichlin S. Plasma growth hormone concentration in the rat determined by radioimmunoassay: influence of sex, pregnancy, lactation, anesthesia, hypophysectomy and extrasellar pituitary transplants. Endocrinology. 1966 Aug;79(2):275–280. doi: 10.1210/endo-79-2-275. [DOI] [PubMed] [Google Scholar]
  21. WASSERMAN E., LEVINE L. Quantitative micro-complement fixation and its use in the study of antigenic structure by specific antigen-antibody inhibition. J Immunol. 1961 Sep;87:290–295. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES