A Scj1p homolog and folding catalysts present in dog pancreas microsomes

被引:39
作者
Bies, C [1 ]
Guth, S [1 ]
Janoschek, K [1 ]
Nastainczyk, W [1 ]
Volkmer, J [1 ]
Zimmermann, R [1 ]
机构
[1] Univ Saarlandes, D-66421 Homburg, Germany
关键词
endoplasmic reticulum; Hsp70; proteins; Hsp40; peptidylprolyl-cis/trans-isomerases; protein disulfide isomerases;
D O I
10.1515/BC.1999.149
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Dog pancreas microsomes represent the key components of the established model system for the analysis of protein transport into the mammalian endoplasmic reticulum. More recently, these microsomes were also employed in cell-free systems which address questions related to protein folding and protein degradation in the mammalian endoplasmic reticulum. In order to get at a complete picture of these undoubtedly related processes in the in vitro system we need to know all the proteins we are dealing with, and their respective stoichiometries. Here we give a progress report on our attempts to identify and to quantify the soluble molecular chaperones and folding catalysts which are present in the lumen of dog pancreas microsomes. Eventually, we will need to know how the in vitro system compares with the situation in intact pancreatic cells as well as in other cells.
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页码:1175 / 1182
页数:8
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