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末端N-乙酰葡糖胺与天冬酰胺连接的寡糖的连接发生在高尔基体堆叠的中央潴泡中。

Attachment of terminal N-acetylglucosamine to asparagine-linked oligosaccharides occurs in central cisternae of the Golgi stack.

作者信息

Dunphy W G, Brands R, Rothman J E

出版信息

Cell. 1985 Feb;40(2):463-72. doi: 10.1016/0092-8674(85)90161-8.

DOI:10.1016/0092-8674(85)90161-8
PMID:3155653
Abstract

Using monoclonal antibodies and electron microscopy, we have localized N-acetylglucosamine transferase I within the Golgi apparatus. This enzyme initiates the conversion of asparagine-linked oligosaccharides to the complex type. We have found that the enzyme is concentrated in the central (or medial) cisternae of the Golgi stack. Cisternae at the cis and trans ends of the Golgi complex appear to lack this protein. These experiments establish a function for the medial portion of the Golgi and imply that the Golgi is partitioned into at least three biochemically and morphologically distinct cisternal compartments.

摘要

利用单克隆抗体和电子显微镜技术,我们已将N-乙酰葡糖胺转移酶I定位在高尔基体中。这种酶启动天冬酰胺连接的寡糖向复合型的转化。我们发现该酶集中在高尔基体堆叠的中央(或中间)潴泡中。高尔基体复合体顺面和反面的潴泡似乎缺乏这种蛋白质。这些实验确定了高尔基体中间部分的功能,并暗示高尔基体被分成至少三个生物化学和形态学上不同的潴泡区室。

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Cell. 1985 Feb;40(2):463-72. doi: 10.1016/0092-8674(85)90161-8.
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