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通过内切型糖苷酶的作用,从链霉菌属OH-11242培养基中的黏液糖蛋白释放具有还原端N-乙酰半乳糖胺的寡糖。

Release of oligosaccharides possessing reducing-end N-acetylgalactosamine from mucus glycoprotein in Streptomyces sp. OH-11242 culture medium through action of endo-type glycosidase.

作者信息

Iwase H, Ishii I, Ishihara K, Tanaka Y, Omura S, Hotta K

机构信息

Department of Biochemistry, School of Medicine, Kitasato University, Kanagawa, Japan.

出版信息

Biochem Biophys Res Commun. 1988 Feb 29;151(1):422-8. doi: 10.1016/0006-291x(88)90610-9.

Abstract

A crude enzyme preparation from a culture medium of Streptomyces sp. OH-11242 contained endo-alpha-N-acetylgalactosaminidase activity. The activity could be induced by the addition of purified porcine gastric mucin to the culture medium. Oligosaccharides corresponding to approximately 2-14 glucose units were detected in the culture medium and also in an incubated reaction mixture of crude enzyme preparation and mucus glycoprotein. The resulting product with N-acetylgalactosamine at the reducing terminal implied the presence of a new type of endo-glycosidase liberating not only Gal beta 1-3GalNAc but also other larger oligosaccharides by hydrolysis of the O-glycosidic linkage between GalNAc and Ser (Thr).

摘要

来自链霉菌属OH-11242培养基的粗酶制剂含有内切α-N-乙酰半乳糖胺酶活性。向培养基中添加纯化的猪胃粘蛋白可诱导该活性。在培养基以及粗酶制剂与粘液糖蛋白的孵育反应混合物中均检测到了对应约2 - 14个葡萄糖单位的寡糖。在还原端带有N-乙酰半乳糖胺的产物表明存在一种新型内切糖苷酶,其通过水解GalNAc与Ser(Thr)之间的O-糖苷键,不仅释放Galβ1-3GalNAc,还释放其他更大的寡糖。

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