Covalent attachment of peptides to membranes for dot-blot analysis of glycosylation sites and epitopes

Anal Biochem. 1993 Jun;211(2):179-82. doi: 10.1006/abio.1993.1253.

Abstract

Noncovalent binding of proteins to membranes is often employed for dot-blot analysis with various visualization techniques. These techniques are usually not applicable to peptide dot-blot analysis due to peptide wash-off during the staining procedure. As exemplified with a synthetic peptide and peptides produced by proteolysis of a protein, it is possible to achieve efficient covalent attachment to Immobilon-AV membranes. The utility of this membrane has been demonstrated with immunostaining and carbohydrate staining procedures.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Collodion
  • Epitopes / analysis*
  • Glycosylation
  • Immunoblotting / methods
  • Membranes, Artificial*
  • Molecular Sequence Data
  • Peptides / analysis*
  • Peptides / immunology
  • Peptides / metabolism
  • Polyvinyls
  • Staining and Labeling / methods

Substances

  • Epitopes
  • Membranes, Artificial
  • Peptides
  • Polyvinyls
  • polyvinylidene fluoride
  • Collodion