Investigation of the allergenicity of beta-lactoglobulin and its cleavage fragments.
Fragments of beta-lactoglobulin were produced by proteolytic cleavage with trypsin, and chemical cleavage with cyanogen bromide, followed by gel filtration on Sephadex G-50. The antigenicity and allergenicity of the products were studied, before and after reductive cleavage by treatment with 2-mercaptoethanol. The former was determined by inhibition ELISA using IgG anti-beta-lactoglobulin raised in rabbits, whilst the latter was determined by inhibition ELISA and mast cell challenge, using respectively the sera and peritoneal cells of rats experimentally sensitised to beta-lactoglobulin. The findings raise interesting points about the structural basis of allergenicity in relation to antigenicity.
Q
Q
Huang
J W
JW
Coleman
D R
DR
Stanworth
D000485:Allergens; D000818:Animals; D001667:Binding, Competitive; D004220:Disulfides / Q000378:metabolism; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes; D007073:Immunoglobulin E / Q000276:immunology; D007074:Immunoglobulin G / Q000276:immunology; D007782:Lactoglobulins / Q000276:immunology* / Q000494:pharmacology; D008297:Male; D008407:Mast Cells / Q000378:metabolism; D010446:Peptide Fragments / Q000276:immunology* / Q000494:pharmacology; D011817:Rabbits; D051381:Rats; D012701:Serotonin / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
D000485:Allergens; D004220:Disulfides; D000939:Epitopes; D007074:Immunoglobulin G; D007782:Lactoglobulins; D010446:Peptide Fragments; D012701:Serotonin; D007073:Immunoglobulin E; D014357:Trypsin