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对接蛋白在糙面内质网的定位:大鼠肝脏中的免疫细胞化学定位

Restriction of docking protein to the rough endoplasmic reticulum: immunocytochemical localization in rat liver.

作者信息

Hortsch M, Griffiths G, Meyer D I

出版信息

Eur J Cell Biol. 1985 Sep;38(2):271-9.

PMID:4043092
Abstract

Docking protein (or SRP receptor) is an integral membrane protein essential for translocation of nascent polypeptides across the membrane of the endoplasmic reticulum (ER). Anti-docking protein antibodies were used to localize this protein in situ in thin frozen sections using protein A-gold detection methods. The majority of gold particles was restricted to ribosome-studded membranes, whereas particles were rarely seen in areas rich in smooth ER. Quantitative evaluation of labeling suggests that there is one molecule of docking protein for roughly 10 to 20 bound ribosomes. On the basis of these results we conclude that docking protein is the first functionally-characterized integral marker protein specific for the rough membranes of ER.

摘要

对接蛋白(或信号识别颗粒受体)是一种整合膜蛋白,对于新生多肽跨内质网(ER)膜的转运至关重要。利用蛋白A-金检测方法,抗对接蛋白抗体被用于在薄冰冻切片中原位定位该蛋白。大多数金颗粒局限于布满核糖体的膜上,而在富含光滑内质网的区域则很少见到颗粒。标记的定量评估表明,大约每10到20个结合的核糖体有一个对接蛋白分子。基于这些结果,我们得出结论,对接蛋白是首个功能特性明确的内质网粗面膜特异性整合标记蛋白。

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