Partial characterization of an allergenic glycoprotein from peanut (Arachis hypogaea L.).
A concanavalin A-reactive glycoprotein allergen has been isolated from peanut (Arachis hypogaea). The allergen was separated by affinity chromatography and purified by gel permeation and ion-exchange chromatography. The monomeric molecular weight is 65,000 and the pI is 4.6. The presence of one cysteine residue per molecule results in some dimer formation. Concanavalin A-reactive glycoprotein is a potent allergen for peanut-sensitive patients in both in vivo and in vitro tests. It is allergenically stable, on in vitro examination, at temperatures of up to 100 degrees C and over the pH range 2.8-10. Removal of the carbohydrate moiety failed to eliminate the allergenicity. Concanavalin A-reactive glycoprotein is identified in the crossed immunoelectrophoretic pattern as a major antigen of peanut protein extract but its structural characteristics indicate that it is probably not a component of the major storage-protein complex, arachin.
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Howden
D000485:Allergens / Q000302:isolation & purification*; D000596:Amino Acids / Q000032:analysis; D010367:Arachis / Q000032:analysis* / Q000276:immunology; D002241:Carbohydrates / Q000032:analysis; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003208:Concanavalin A; D006023:Glycoproteins / Q000276:immunology / Q000302:isolation & purification*; D006801:Humans; D007123:Immunoelectrophoresis, Two-Dimensional; D007073:Immunoglobulin E / Q000276:immunology; D007428:Intradermal Tests; D008970:Molecular Weight; D037121:Plant Lectins; D010940:Plant Proteins / Q000276:immunology / Q000302:isolation & purification*; D011852:Radioallergosorbent Test
D000485:Allergens; D000596:Amino Acids; D002241:Carbohydrates; D006023:Glycoproteins; D037121:Plant Lectins; D010940:Plant Proteins; D003208:Concanavalin A; D007073:Immunoglobulin E