Abstract
We have examined the lectinlike properties of pertussis toxin by binding-inhibition assays and affinity chromatography of goose erythrocyte membranes. Although pertussis toxin and wheat germ agglutinin apparently recognize similar sugar sequences on glycoproteins, the binding activities of the two lectins are not identical.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Acetylglucosamine
-
Animals
-
Binding, Competitive
-
Erythrocyte Membrane / metabolism
-
Geese
-
Lectins / pharmacology*
-
Molecular Weight
-
Pertussis Toxin*
-
Receptors, Mitogen / analysis
-
Sialoglycoproteins / metabolism
-
Virulence Factors, Bordetella / metabolism
-
Virulence Factors, Bordetella / pharmacology*
-
Wheat Germ Agglutinins / metabolism
Substances
-
Lectins
-
Receptors, Mitogen
-
Sialoglycoproteins
-
Virulence Factors, Bordetella
-
Wheat Germ Agglutinins
-
wheat germ agglutinin receptor
-
Pertussis Toxin
-
Acetylglucosamine