Parvalbumin, a cross-reactive fish allergen, contains IgE-binding epitopes sensitive to periodate treatment and Ca2+ depletion

This publication has 26 references indexed in Scilit:

• Fish allergy: Evaluation of the importance of cross-reactivity
  The Journal of Pediatrics, 1992
• Homology of Two cDNAs Coding for Birch Pollen Allergens with Calmodulin: Protein-Bound Ca2+ Affects the IgE-Binding Capacity
  International Archives of Allergy and Immunology, 1992
• Ionic interactions with parvalbumins
  Journal of Molecular Biology, 1991
• A follow‐up study of children with food allergy. Clinical course in relation to serum IgE‐ and IgG‐antibody levels to milk, egg and fish
  Clinical and Experimental Allergy, 1981
• Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
  Proceedings of the National Academy of Sciences, 1979
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976
• The Primary Structure of the Major Parvalbumin from Hake Muscle. Isolation and General Properties of the Protein
  European Journal of Biochemistry, 1971
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970
• Characterization of a major allergen (cod): Effect of enzymic hydrolysis on the allergenic activity
  Journal of Allergy, 1969
• Studies in food allergy
  Journal of Allergy, 1946