Substrate Specificities of α-N-Acetylgalactosaminidases I and II from Squid Liver
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概要
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The substrate specificities of the squid liver α-N-acetylgalactosaminidases I and II were studied with natural compounds containing α-N-acetylgalactosaminyl or other glycosyl terminals as substrates. Both α-N-acetylgalactosaminidases I and II hydrolyzed terminal α-N-acetyl-galac-tosaminyl linkages of the natural compounds investigated; asialo bovine submaxillary mucin, Forssman glycolipid, human ovarian cyst A-glycoprotein and blood group A-type ghosts. On the other hand, the oligosaccharides containing α-galactosyl terminals, ceramide trihexoside and juman ovarian cyst B-glycoprotein, were hydrolyzed by α-N-acetylgalactosaminidase I but not by α-N-acetylgalactosaminidase II. The milk oligosaccharides with other glycosyl terminals were not hydrolyzed by either enzyme. Application of α-N-acetylgalactosaminidase from squid liver together with other glycosidases was effective in structural studies of Forssman glycolipid.
- 公益社団法人日本薬学会の論文
- 1988-10-25
著者
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梨田(旧姓伊藤) 智子
Department Of Health Chemistry Niigata College Of Pharmacy
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宇田 裕
Department of Health Chemistry, Niigata College of Pharmacy
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白石 隆幸
Laboratory Of Health Chemistry Niigata College Of Pharmacy
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宇田 裕
Department Of Health Chemistry Niigata College Of Pharmacy
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白石 隆幸
Department of Health Chemistry, Niigata College of Pharmacy
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