“Active” two-dimensional electrophoresis of rat liver DNA-polymerase α

1997 ◽  
Vol 18 (3-4) ◽  
pp. 553-556 ◽  
Author(s):  
Stanislav N. Naryzhny
Keyword(s):  
Dna Polymerase ◽  
Rat Liver ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dna Polymerase Α ◽  
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.

Sialic Acid Dependent Polypeptide Chain Heterogeneity of Human Fibrinogen Demonstrated by Two-Dimensional Electrophoresis

1982 ◽  
Vol 47 (01) ◽  
pp. 019-021 ◽  
Author(s):  
Cemal Kuyas ◽  
André Haeberli ◽  
P Werner Straub
Keyword(s):  
Sialic Acid ◽  
Polypeptide Chain ◽  
Two Dimensional ◽  
Charge Heterogeneity ◽  
Human Fibrinogen ◽  
Two Dimensional Electrophoresis ◽  
Isoelectric Points ◽  
Polypeptide Chains ◽  
Dimensional Electrophoresis ◽  
Chain Type

SummaryHuman fibrinogen was compared with asialofibrinogen by two-dimensional electrophoresis to evaluate the contribution of sialic acid to the heterogeneity of the γ- and Bβ-polypeptide chains.Reduced fibrinogen showed three major variants for both the γ- and Bβ-chains. In addition two minor γ-bands with a more acidic isoelectric point than the normal γ-chains were observed. Electrophoresis in the second dimension (SDS) suggests that these most acidic bands are γ-chain-variants with a higher molecular weight. In asialofibrinogen only two predominant variants with more alkaline isoelectric points were present in each chain type.It is concluded that enzymatic removal of sialic acid partially reduces the heterogeneity of the γ- and Bβ-polypeptide chains of human fibrinogen, but additional sources producing charge heterogeneity must be sought.

Improvement of Two-dimensional Electrophoresis of Rice (Oryza sativaL.) Proteomics

2012 ◽  
Vol 18 (5) ◽  
pp. 819 ◽  
Author(s):  
Yanhua YANG ◽  
Weitong CUI ◽  
Xiaoyong LIU ◽  
Keming ZHU ◽  
Keping CHEN
Keyword(s):  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis
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