Improvements in two-dimensional gel electrophoresis by utilizing a low cost “in-house” neutral pH sodium dodecyl sulfate-polyacrylamide gel electrophoresis system

PROTEOMICS ◽  
2005 ◽  
Vol 5 (9) ◽  
pp. 2309-2314 ◽  
Author(s):  
David R. M. Graham ◽  
Christopher P. Garnham ◽  
Qin Fu ◽  
Jeffrey Robbins ◽  
Jennifer E. Van Eyk
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Low Cost ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Neutral Ph ◽  
Electrophoresis System

A New Method for Proteome Screening with Two-Dimensional Urea-Sds Polyacrylamide Gel Electrophoresis

2014 ◽  
Vol 1 (1) ◽  
Author(s):  
Areeba Ahmad ◽  
Riaz Ahmad
Keyword(s):  
Gel Electrophoresis ◽  
Protein Separation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cost Effective ◽  
Polyacrylamide Gel ◽  
Present System ◽  
Liver Protein ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

AbstractTwo-dimensional gel electrophoresis (2DE) separating proteins on the basis of their pI and molecular mass remain the best available technique for protein separation and characterization to date. But due to several limitations, including streak formation in IEF gels, partial solubility of proteins, expensive running conditions and relatively longer time taken, a simple urea-SDS-2D polyacrylamide gel electrophoresis (US2DE) is described here. The system is reasonably sensitive, cost effective with good reproducibility. The method described in this paper employs a chaotropic agent, urea, in the first dimension and sodium dodecyl sulphate (SDS), like conventional system, in the second dimension with an addition of polyacrylamide to screen the liver proteome of healthy and chemically induced fibrotic rats. The system separates the protein on the basis of chargeto- mass ratio and clearly demonstrates differential expression in the liver protein repertoire of healthy and fibrotic rats. Moreover, the present system, like other 2D electrophoretic procedures revealed at least 22 novel spots in the investigated tissues. The technique may be utilized for comprehensive proteome screening of any biological sample and would provide an overview to narrow down the candidate proteins or biomarkers.

scholarly journals A novel two-dimensional polyacrylamide-gel pattern, which may be due to allelic genes, of phenylalanine hydroxylase in monkeys

1985 ◽  
Vol 231 (1) ◽  
pp. 197-199 ◽  
Author(s):  
S C Smith ◽  
W McAdam ◽  
R G H Cotton ◽  
J F B Mercer
Keyword(s):  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Phenylalanine Hydroxylase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
The Novel ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Monkey Liver

Two-dimensional gel electrophoresis of immunopurified monkey liver phenylalanine hydroxylase showed a novel form of the enzyme, in 4 out of 24 monkeys, in which each polypeptide spot was split into a doublet with the same charge but slightly different mobility in the sodium dodecyl sulphate/polyacrylamide-gel-electrophoresis (as opposed to the isoelectric-focusing) dimension. Phenylalanine hydroxylase formed by translation of RNA from a liver containing the novel form showed the doublet pattern, suggesting that it is due to differences in mRNA. By analogy with the rat, this mRNA difference could be due to allelic genes.

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