Differential time-course of induction of rat liver gamma-glutamyltransferase and drug-metabolizing enzymes in the endoplasmic reticulum, golgi and plasma membranes after a single phenobarbital injection. Evaluation of protein variations by two-dimensional electrophoresis

1987 ◽  
Vol 5 (3) ◽  
pp. 217-231 ◽  
Author(s):  
B. Antoine ◽  
A. Rahimi-Pour ◽  
G. Siest ◽  
J. Magdalou ◽  
M. M. Galteau
Keyword(s):  
Endoplasmic Reticulum ◽  
Rat Liver ◽  
Time Course ◽  
Plasma Membranes ◽  
Drug Metabolizing Enzymes ◽  
Two Dimensional ◽  
Metabolizing Enzymes ◽  
Gamma Glutamyltransferase ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

scholarly journals Identification of protein disulphide-isomerase as a major acidic polypeptide in rat liver microsomal membranes

1983 ◽  
Vol 213 (1) ◽  
pp. 245-248 ◽  
Author(s):  
E N C Mills ◽  
N Lambert ◽  
R B Freedman
Keyword(s):  
Liver Enzyme ◽  
Rat Liver ◽  
Peptide Mapping ◽  
Bovine Liver ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Protein Disulphide Isomerase ◽  
Two Dimensional Electrophoresis ◽  
Microsomal Membranes ◽  
Dimensional Electrophoresis

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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