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伴刀豆球蛋白A与刀豆α-D-甘露糖苷酶天然形式和变性形式的相互作用。

Interaction of concanavalin A with native and denatured forms of jackbean alpha-D-mannosidase.

作者信息

Bowles D J, Chaplin M F, Marcus S E

出版信息

Eur J Biochem. 1983 Feb 15;130(3):613-8. doi: 10.1111/j.1432-1033.1983.tb07193.x.

Abstract

Tetrameric alpha-D-mannosidase from jackbean is a glycoprotein containing at least one mannosylated oligosaccharide. In the native enzyme, the oligosaccharide is sterically masked from interaction with either endoglucosaminidase H or concanavalin A. Denaturation into subunits permits endoglucosaminidase hydrolysis and removal of the oligosaccharide. The mannosyl residues are attached only to the heavy type of subunit. Removal of the oligosaccharide(s) from the denatured heavy subunit requires the joint action of both alpha-D-mannosidase and N-acetyl-beta-D-glucosaminidase.

摘要

来自刀豆的四聚体α-D-甘露糖苷酶是一种糖蛋白,含有至少一种甘露糖基化寡糖。在天然酶中,寡糖在空间上被遮蔽,无法与内切葡糖胺酶H或伴刀豆球蛋白A相互作用。变性成亚基后,内切葡糖胺酶可进行水解并去除寡糖。甘露糖残基仅连接到重链型亚基上。从变性的重链亚基上去除寡糖需要α-D-甘露糖苷酶和N-乙酰-β-D-葡糖胺酶的共同作用。

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