Endoglycosidases acting on carbohydrate moieties of glycoproteins: demonstration in mammalian tissue.
Endoglycosidases acting on carbohydrate moieties of glycoproteins: demonstration in mammalian tissue.
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作用于糖蛋白碳水化合物部分的内切糖苷酶：在哺乳动物组织中的演示。
DOI：
10.1016/s0006-291x(74)80027-6
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发表时间：
1974
影响因子：
3.1
通讯作者：
A. Kobata
中科院分区：
文献类型：
--
作者：
M. Nishigaki;T. Muramatsu;A. Kobata
大鼠和猪器官的酶制剂从[14 C]-乙酰-Asn（GlcNAc）2（Man）6释放[14 C]-乙酰-AsnGlcNAc，无中间产物，表明存在作用于底物的糖苷内切酶。采用SephadexG-200柱层析从猪肝中分离α-甘露糖苷酶。纯化的酶的底物特异性似乎是独特的，因为它只水解几种糖肽及其衍生物中的卵清蛋白糖肽。
Enzyme preparations from rat and porcine organs released [14C]-acetyl-AsnGlcNAc from [14C]-acetyl-Asn(GlcNAc)2(Man)6without intermediate products, indicating the presence of an endoglycosidase acting on the substrate. The enzyme from porcine liver was separated from α-mannosidase by Sephadex G-200 column chromatography. The substrate specificity of the purified enzyme appears to be unique, since it hydrolyzed only ovalbumin glyco-peptides among several glycopeptides and their derivatives.