78 ホヤ抗原(Gi-rep)の糖鎖構造と抗原活性

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Sea-squirt asthma is an allergic disease found in the workers of oyster farm in Hiroshima Bay. This allergy is induced by inhalation of spray of body fluid from sea-squirt which grows on oyster shells. Recently, we have isolated three acidic glycoproteins (Gi-rep, Ei-M, DIIIa) as the antigens specific to the allergy. It was also suggested that a certain carbohydrate moiety of the antigens acted as the antigenic determinant specific to the allergy. Thus, the structure of carbohydrate chains of an isolated antigen, Gi-rep, was examined in relation to the antigenic activity. 1. Two glycopeptides (Gp-1, Gp-2) were fractionated from a Pronase digest of Gi-rep. Both were still antigenically active as examined in vivo by skin test against the allergic patients, though the in vitro activities detected by RIA were relatively low. 2. An alkaline treatment on Gp-1 (larger molecule) gave antigenically active oligosaccharides originated from O-glycosidic chains of Gp-1. MS-analysis showed that they were branched saccharides having GalNAc at the non-reducing terminal. 3. Somewhat larger carbohydrate unit (DP ca. 30) having antigenic activity was obtained from Gp-2 (smaller molecule) by the alkaline treatment. MS-analysis showed again that it was a branched saccharide having GalNAc at the non-reducing terminal. 4. The antigenic activity and the terminal GalNAc were simultaneously eliminated from Gp-2 by periodate oxidation. However, subsequent Smith Degradation recovered the antigenic activity and the terminal GalNAc from core structure of the oxidized product.
天然有機化合物討論会の論文
1985-09-07

78 ホヤ抗原(Gi-rep)の糖鎖構造と抗原活性

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