Isolation, purification and characterization of beta-hCGRP from human spinal cord

Biochem Biophys Res Commun. 1990 Mar 30;167(3):993-1000. doi: 10.1016/0006-291x(90)90621-s.

Abstract

Human beta-calcitonin gene-related peptide (beta-hCGRP) was isolated and purified from spinal cord. The complete characterization of this material was based on definitive mass analysis by fast atom bombardment mass spectrometry together with gas phase sequencing. Combining these data we have characterized the structure of beta-hCGRP including the C-terminal sequence, the presence of the S-S bridge and of phenylalanineamide as the C-terminal amino acid, and fully confirmed the amino acid sequence predicted from the nucleotide analysis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Calcitonin Gene-Related Peptide / isolation & purification*
  • Chromatography, Gel
  • Cyanogen Bromide
  • Disulfides / analysis
  • Freeze Drying
  • Gas Chromatography-Mass Spectrometry
  • Humans
  • Molecular Sequence Data
  • Peptide Fragments / isolation & purification
  • Radioimmunoassay
  • Radioligand Assay
  • Spinal Cord / analysis*

Substances

  • Disulfides
  • Peptide Fragments
  • Calcitonin Gene-Related Peptide
  • Cyanogen Bromide