参与O-连接寡糖合成的两种酶定位于小鼠淋巴瘤BW5147细胞中不同密度的膜上。
Two enzymes involved in the synthesis of O-linked oligosaccharides are localized on membranes of different densities in mouse lymphoma BW5147 cells.
作者信息
Elhammer A, Kornfeld S
出版信息
J Cell Biol. 1984 Jul;99(1 Pt 1):327-31. doi: 10.1083/jcb.99.1.327.
Abstract
Microsomal membranes from mouse lymphoma BW5147 cells were fractionated on a continuous sucrose gradient and assayed for two enzymes involved in the synthesis of O-linked oligosaccharides. Both enzymes were recovered in membranes that were less dense than the membranes containing the endoplasmic reticulum marker enzymes, glucosidase I and II. UDP-Gal:N-acetylgalactosamine-beta 1, 3-galactosyltransferase had a distribution that coincided with that of the galactosyltransferase that acts on asparagine-linked oligosaccharides. This latter enzyme has been immunolocalized to the trans Golgi elements. The UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferase was recovered in a membrane fraction of intermediate density, between the endoplasmic reticulum and trans Golgi markers. These findings are consistent with the assembly of O-linked oligosaccharides occurring in at least two different Golgi compartments.
摘要
从小鼠淋巴瘤BW5147细胞中提取的微粒体膜在连续蔗糖梯度上进行分级分离，并对参与O-连接寡糖合成的两种酶进行测定。两种酶都在比含有内质网标记酶（葡糖苷酶I和II）的膜密度更低的膜中回收。UDP-半乳糖：N-乙酰半乳糖胺-β1,3-半乳糖基转移酶的分布与作用于天冬酰胺连接寡糖的半乳糖基转移酶的分布一致。后一种酶已通过免疫定位到反式高尔基体元件。UDP-GalNAc：多肽N-乙酰半乳糖胺基转移酶在中间密度的膜组分中回收，介于内质网和反式高尔基体标记物之间。这些发现与O-连接寡糖的组装发生在至少两个不同的高尔基体区室中一致。
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