Department of Biology, C-016, University of California, San Diego, La Jolla, California 92093.
Plant Physiol. 1985 Aug;78(4):835-8. doi: 10.1104/pp.78.4.835.
The transport and accumulation of phytohemagglutinin in developing bean (Phaseolus vulgaris L.) cotyledons is accompanied by the transient presence of N-acetylglucosamine (GlcNAc) residues on the oligosaccharide sidechains of this glycoprotein. These peripheral GlcNAc residues can be distinguished from those in the chitobiose portion of the oligosaccharide sidechains by their sensitivity to removal by the exoglycosidase beta-N-acetylglucosaminidase. GlcNAc residues sensitive to removal by beta-N-acetylglucosaminidase are present not only on phytohemagglutinin, but also on other newly synthesized proteins. The enzyme UDPGlcNAc:glycoprotein GlcNAc-transferase which transfers GlcNAc residues to glycoproteins was first described by Davies and Delmer (Plant Physiol 1981 68: 284-291). The data presented here show that this enzyme is associated with the Golgi complex of developing cotyledons.
在发育中的菜豆(Phaseolus vulgaris L.)子叶中,血凝素的运输和积累伴随着该糖蛋白的寡糖侧链上 N-乙酰葡萄糖胺(GlcNAc)残基的短暂存在。这些外周 GlcNAc 残基可通过其对糖苷酶β-N-乙酰氨基葡萄糖苷酶的敏感性与寡糖侧链中壳二糖部分的 GlcNAc 残基区分开来。对β-N-乙酰氨基葡萄糖苷酶敏感的 GlcNAc 残基不仅存在于血凝素上,也存在于其他新合成的蛋白质上。首先由 Davies 和 Delmer(植物生理学 1981 68:284-291)描述的将 GlcNAc 残基转移到糖蛋白上的酶 UDPGlcNAc:糖蛋白 GlcNAc 转移酶。这里呈现的数据表明,这种酶与发育中的子叶的高尔基体复合物相关。