负责多核糖体附着于大鼠肝脏粗面微粒体部分的膜蛋白的分离与鉴定。
Isolation and characterization of membrane proteins responsible for attachment of polyribosomes to rough microsomal fraction of rat liver.
作者信息
Fujita S, Ogata F, Nakamura J, Omata S, Sugano H
出版信息
Biochem J. 1977 Apr 15;164(1):53-66. doi: 10.1042/bj1640053.
Abstract
A protein fraction which has a high affinity for polyribosomes was isolated from rough microsomal membranes of rat liver. The mode of polyribosome binding to this fraction (R-fraction) was studied by using CsCl equilibrium centrifugation and compared with that for stripped rough microsomal membranes. The following were found. (1) The polyribosome-binding cpacity of the R-fraction was heat-labile and sensitive to trypsin, and was suppressed by increasing KCl concentration and addition of 0.1 mM-aurintricarboxylic acid. (2) Of the four subfractions obtained by gel filtration of the R-fraction on a Sephadex G-200, only the R1-fraction, eluted at the void volume, showed a high affinity for polyribosomes. The polyribosome-binding capacity of the R1-fraction decreased with time on storage at 4 degrees C. (3) The R1-fraction contained three major proteins with mol. wts. 108,000, 99,000 and 65,000.
摘要
从大鼠肝脏的粗面微粒体膜中分离出一种对多核糖体具有高亲和力的蛋白质组分。通过氯化铯平衡离心研究了多核糖体与该组分（R组分）的结合方式，并与脱蛋白粗面微粒体膜的结合方式进行了比较。发现如下：（1）R组分的多核糖体结合能力对热不稳定且对胰蛋白酶敏感，并且随着氯化钾浓度的增加和添加0.1 mM金精三羧酸而受到抑制。（2）通过在葡聚糖凝胶G-200上对R组分进行凝胶过滤获得的四个亚组分中，只有在空体积处洗脱的R1组分对多核糖体具有高亲和力。R1组分的多核糖体结合能力在4℃储存时随时间下降。（3）R1组分包含三种主要蛋白质，分子量分别为108,000、99,000和65,000。
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