Bovine brain S100 proteins: separation and characterization of a new S100 protein species

J Neurochem. 1983 Jan;40(1):145-52. doi: 10.1111/j.1471-4159.1983.tb12664.x.

Abstract

Three S100 protein species (S100a, S100b, S100a') have been purified from bovine brain using a modification of standard preparative methods. A higher yield for each protein was obtained at the last separation step. Characterization by urea/sodium dodecyl sulfate/polyacrylamide gel electrophoresis, UV absorption spectra, and fluorescence parameters provided evidence of a new tryptophan-containing S100 protein called S100a', which exhibits, as S100a and S100b, the properties of a Ca2+ binding protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biomarkers*
  • Brain Chemistry*
  • Calcium
  • Cattle
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Immunodiffusion
  • Molecular Weight
  • Nerve Growth Factors
  • Nerve Tissue Proteins / isolation & purification*
  • Peptide Fragments / analysis
  • S100 Calcium Binding Protein beta Subunit
  • S100 Proteins / isolation & purification*
  • Spectrophotometry, Ultraviolet

Substances

  • Biomarkers
  • Nerve Growth Factors
  • Nerve Tissue Proteins
  • Peptide Fragments
  • S-100 calcium-binding protein alpha subunit
  • S100 Calcium Binding Protein beta Subunit
  • S100 Proteins
  • Calcium