卵アレルギー患者血清によるIgE結合卵白抗原の検索 : ニワトリ,ウズラ,アヒル卵の主要タンパク質について

IgE binding antigen of the major proteins in egg white, which is hen (H), quail (Q) and duck (D) was determined using the sera of patients with egg allergy. The major proteins of egg white were ovotransferrin (OT), ovoinhibitor (OI), ovalbumin (OA), ovomucoid (OM) and lysozyme (LY). The age of egg allergy patients is used this present studey were 3 years 4 months-old to 4 months-old (RAST 2～6). After SDS-PAGE analysis of egg whites, Western-blotting and enzyme-immunoassay was examined using the serum of 33 patoents with egg allergy. The positive blots of IgE binding proteins were ranked score 1～5 by positive color. The blots from score 2 to score 5 were positive of IgE binding. The positive percent of IgE blotting to hen OM was shown to have higher positive percent relatively to the other major proteins with the serum of 33 patients. And, on the sera of RAST 3 and RAST 4～6, ratio of IgE binding to hen OM indicated high positive percent. Therefore, from this study, these findings suppose that hen OM is the most important allergen of egg white proteins

魚類アレルゲンの分離とその性質

Salt-soluble fractions (I, II) , an alkali-soluble fraction (III) and an acid-soluble fraction (IV) were separated from fresh Cod (Gadus macrocephalus). Allergenic activities of the I～IV fractions were measured using mAb parvalbumin (mAb PV) and sera of fish-allergy patients. 36kDa and 12.3kDa proteins of the fractions showed a positive reaction against mAb PV. It was presumed that the 12.3kDa protein was parvalbumin (PV) judging from references. However, a positive reaction was indicated only in the 36kDa protein of the III fraction in the IgE reaction with a fish-allergy patient serum. Therefore, it was presumed that the patient having the above serum developed an allergy to a protein being different from PV. Moreover, it was presumed that the 36kDa allergen has the immunity intersection to PV because the positive reaction was shown against mAb PV. Allergenic activities of alkali-soluble fractions (III) from Salmon, (Oncorhynchus keta), Saury, (Cololabis saira), Sardine (Sardinops melanostictus), Flatfish (Pleuronectes herzensteini) were measured with mAb PV and the sera of the patients. However, a clear allergen was not observed as compared with the Cod III fraction. The Cod III fraction in the acidic solution (pH2～6) was decreased about 50% binding activity with mAb PV by heating at 100℃. The activity of the same fraction in the alkaline solution (pH7～10) was not decreased. Therefore, the Cod III fraction was considered to be heat-stable in the alkaline solution