Two-dimensional electrophoresis of membrane proteins factors affecting resolution of rat-liver microsomal proteins

1983 ◽  
Vol 734 (2) ◽  
pp. 160-167 ◽  
Author(s):  
E.N.Clare Mills ◽  
Robert B. Freedman
Author(s):  
Philip W. Pemberton ◽  
Robert W. Lobley ◽  
Raymond Holmes ◽  
Susanne H. Sørensen ◽  
Kenneth W. Simpson ◽  
...  

2007 ◽  
Vol 389 (4) ◽  
pp. 1033-1045 ◽  
Author(s):  
Ralf J. Braun ◽  
Norbert Kinkl ◽  
Monika Beer ◽  
Marius Ueffing

1983 ◽  
Vol 213 (1) ◽  
pp. 245-248 ◽  
Author(s):  
E N C Mills ◽  
N Lambert ◽  
R B Freedman

Protein disulphide-isomerase was purified to homogeneity from rat liver by a rapid high-yielding procedure. Structural properties of the pure enzyme were very similar to those of the bovine liver enzyme purified by the same method. The purified rat liver enzyme was subjected to two-dimensional gel electrophoresis in the presence and in the absence of microsomal membranes, and shown to co-electrophorese with a major acidic polypeptide clearly identifiable in the two-dimensional electrophoretic profile of microsomal membranes. This identification was confirmed by peptide ‘mapping’ of the pure enzyme and of the defined spot from a two-dimensional electrophoresis gel.


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