Complete amino acid sequence of human vitamin D-binding protein (group-specific component): evidence of a three-fold internal homology as in serum albumin and alpha-fetoprotein

Biochim Biophys Acta. 1986 Jun 5;871(2):189-98. doi: 10.1016/0167-4838(86)90173-1.

Abstract

The complete amino acid sequence (458 amino acid residues) of human group-specific component 2 (Gc2) protein was determined. Computer analyses established a three-fold internal homology of Gc2 protein as well as an extensive homology between the overall structures of Gc2 protein, human serum albumin and human alpha-fetoprotein.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Chromatography, High Pressure Liquid
  • Cyanogen Bromide
  • Endopeptidases
  • Humans
  • Peptide Fragments
  • Serine Endopeptidases*
  • Serum Albumin*
  • Trypsin
  • Vitamin D-Binding Protein*
  • alpha-Fetoproteins*

Substances

  • Peptide Fragments
  • Serum Albumin
  • Vitamin D-Binding Protein
  • alpha-Fetoproteins
  • Endopeptidases
  • Serine Endopeptidases
  • glutamyl endopeptidase
  • Trypsin
  • Cyanogen Bromide