Applications of chemical cleavage procedures to the peptide mapping of neurofilament triplet protein bands in sodium dodecyl sulfate-polyacrylamide gel electrophoresis

Anal Biochem. 1986 Apr;154(1):171-82. doi: 10.1016/0003-2697(86)90511-7.

Abstract

A procedure for examining possible sequence homology in the triplet neurofilament proteins using a sodium dodecyl sulfate-polyacrylamide gel electrophoresis system is described. Five different chemical reagents (cyanogen bromide, BNPS-skatole, hydroxylamine, formic acid, and nitrothiocyanobenzoic acid) have been used for peptide mapping studies. Potential applications of this technique are discussed.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Cyanogen Bromide
  • Electrophoresis, Polyacrylamide Gel / methods*
  • Formates
  • Hydroxylamine
  • Hydroxylamines
  • Intermediate Filament Proteins / isolation & purification*
  • Neurofilament Proteins
  • Peptide Fragments / isolation & purification*
  • Skatole / analogs & derivatives
  • Sodium Dodecyl Sulfate
  • Thiocyanates

Substances

  • Formates
  • Hydroxylamines
  • Intermediate Filament Proteins
  • Neurofilament Proteins
  • Peptide Fragments
  • Thiocyanates
  • formic acid
  • BNPS-skatole
  • Hydroxylamine
  • Sodium Dodecyl Sulfate
  • Skatole
  • 2-nitro-5-thiocyanobenzoic acid
  • Cyanogen Bromide