Literature DB >> 604288

Human somatotropin 53. Synthesis and biological activity of the amino terminal fifty-four residue fragment.

R L Noble, D Yamashiro, C H Li.   

Abstract

The amino terminal 54 residue peptide fragment of human somatotropin [Cys(Gam)53]-HGH-(1-54), has been synthesized by the solid-phase method. The symmetrical anhydride and active ester coupling methods were used exclusively. The synthetic product was purified by gel fitration isoelectric focusing, and partition chromatography. It was found to be homogeneous by six additional criteria. In complement fixation experiments the synthetic product was immunologically active with antisera to HGH and [cys(Cam)53]-HGH-(134). Antiserum raised against the synthetic product was immunologically active in the homologous assay and with HGH,[Cys(Cam)53]-HGH-(1-134), and [Cys(Cam)53]-HGH-(15-125). The synthetic fragment exhibited 53% of the activity of [Cys(Cam)53]-HGH-(1-134) in the rat tibia assay.

Entities:  

Mesh:

Substances:

Year:  1977        PMID: 604288

Source DB:  PubMed          Journal:  Int J Pept Protein Res        ISSN: 0367-8377


  3 in total

1.  Noncovalent interaction of the NH2-terminal fragment of human somatotropin with the COOH-terminal fragment of human choriomammotropin to generate growth-promoting activity.

Authors:  C H Li
Journal:  Proc Natl Acad Sci U S A       Date:  1978-04       Impact factor: 11.205

2.  Mechanisms and prevention of trifluoroacetylation in solid-phase peptide synthesis.

Authors:  S B Kent; A R Mitchell; M Engelhard; R B Merrifield
Journal:  Proc Natl Acad Sci U S A       Date:  1979-05       Impact factor: 11.205

Review 3.  Human growth hormone: 1974-1981.

Authors:  C H Li
Journal:  Mol Cell Biochem       Date:  1982-07-07       Impact factor: 3.396

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.