Two-dimensional gel electrophoresis (2-DE) with immobilized pH gradients (IPGs) combined with protein identification by mass spectrometry (MS) is currently the workhorse for proteomics. In spite of promising alternative or complementary technologies (e.g. multidimensional protein identification technology, stable isotope labelling, protein or antibody arrays) that have emerged recently, 2-DE is...

We have previously identified proteins in fractions of culture filtrate ofMycobacterium tuberculosis with the capacity to induce cytokine production in monocytes, by using a technique we defined as "monocyte Western blotting" (immunoblotting). In this series of experiments, we have extended this technique to two-dimensional gel electrophoresis and have identified a novel 58-kDa protein ofM. tub...

The two-dimensional electrophoretic method with silver staining we describe better resolves plasma apolipoproteins (apo) than any procedure previously described. It can be used to screen for abnormalities in apoA-I, apoA-II, apoA-IV, apoC-II, apoC-III, apoD, apoE, and apoH. In addition, this is the first presentation of apoD and apoH on two-dimensional gels. This electrophoretic method will per...

Two-dimensional electrophoresis is still a very valuable tool in proteomics, due to its reproducibility and its ability to analyze complete proteins. However, due to its sensitivity to dynamic range issues, its most suitable use in the frame of biomarker discovery is not on very complex fluids such as plasma, but rather on more proximal, simpler fluids such as CSF, urine, or secretome samples. ...

Quantitative proteomic studies, based on two-dimensional gel electrophoresis, are commonly used to find proteins that are differentially expressed between samples or groups of samples. These proteins are of interest as potential diagnostic or prognostic biomarkers, or as proteins associated with a trait. The complexity of proteomic data poses many challenges, so while experiments may reveal pro...

Two-dimensional gel electrophoresis separates all of the component proteins of the ribosomal subunits of Escherichia coli. This method shows 21 proteins in the 30S, and 34 proteins in the 50S, subunit.

Following the recent demonstration of differences in mRNA species in the Novikoff hepatoma and normal rat liver (2), a search was made for differences in the abun dant cytosol proteins of these tissues as well as of several Morris hepatomas and other rat tissues. With the aid of 2dimensional electrophoresis, it was found that each of the nontumorous tissues had a distinctive pattern of abundant...

MOTIVATION Detection of protein spots in two-dimensional gel electrophoresis images (2-DE) is a very complex task and current approaches addressing this problem still suffer from significant shortcomings. When quantifying a spot, most of the current software applications include a lot of background due to poor segmentation. Other software applications use a fixed window for this task, resulting...

In proteomic research, two-dimensional electrophoresis (2-D) is an important tool for investigating differential patterns of qualitative and quantitative protein expression. The strength of the technique is due to its unrivalled power of being able to separate simultaneously thousands of proteins. The key to the comparison of 2-D protein profiles, however, lies in the use of a fast and robust i...