Covalent attachment of peptides to membranes for dot-blot analysis of glycosylation sites and epitopes.
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.
Canas
B
B
Center for Advanced Biotechnology and Medicine, Piscataway, New Jersey 08854.
Dai
Z
Z
Lackland
H
H
Poretz
R
R
Stein
S
S
D000595:Amino Acid Sequence; D001665:Binding Sites; D003101:Collodion; D000939:Epitopes / Q000032:analysis*; D006031:Glycosylation; D015151:Immunoblotting / Q000379:methods; D008567:Membranes, Artificial; D008969:Molecular Sequence Data; D010455:Peptides / Q000032:analysis* / Q000276:immunology / Q000378:metabolism; D011145:Polyvinyls; D013194:Staining and Labeling / Q000379:methods; D005465:Fluorocarbon Polymers
D003101:Collodion; D000939:Epitopes; D008567:Membranes, Artificial; D010455:Peptides; D011145:Polyvinyls; C024865:polyvinylidene fluoride; D005465:Fluorocarbon Polymers