Isolation and Properties of Allergenic Proteins in the Oyster <i>Crassostrea gigas</i>

Abstract

Two allergens, designated as Cra gs 1 and 2, were isolated from the oyster Crassostrea gigas by gel permeation chromatography on a Sephacryl S-300, ion-exchange FPLC on a Mono Q HR 5/5, and reverse-phase HPLC on a TSKgel Phenyl 5PW-RP. Although both allergens were sepFarated from each other by ion-exchange FPLC, they showed the same behaviors in gel permeation chromatography and reverse-phase HPLC. In addition, Cra gs were quite similar to each other as follows: they were 86 kDa glycoproteins with a carbohydrate content of about 5%; they were composed of 35 kDa subunits; they were remarkably abundant in Glx, followed by Asx, Ala, and Leu, and were devoid of Pro and Trp; their reactivities against the sera from seafood allergy patients were equivalent. The molecular masses and characteristics of amino acid composition strongly suggested that Cra gs aretropomyosin of C. gigas.