Gel electrophoresis analysis

G. Muyzer, E. C. de Waal, and A. G. Uitterlinden, Profiling of complex microbial populations by denaturing gradient gel electrophoresis analysis of polymerase chain reaction-amplified genes coding for I6S rRNA. Appl. Environ. Microbiol. 59 695 (1993). 

Carboni L, Piubelli C, Righetti PG, Jansson B, Domenici E. 2002. Proteomic analysis of rat brain tissue comparison of protocols for two-dimensional gel electrophoresis analysis based on different solubilizing agents. Electrophoresis 23 ... 

Fig. 4. Massive production of green fluorescent protein (GFP) by the continuous-flow cell-free method. Sodium dodecyl sulfide-polyacrylamide gel electrophoresis analysis of GFP produced during 14 d of reaction. mRNA produced by transcription of circular plasmid of Ehime University (pEU) was used for the translation reaction in the dialysis membrane system and was added every 48 h. A 0.1 -pL aliquot of the mixture was run on the gel and protein bands were stained with Coomassie Brilliant Blue. The arrow shows GFP and st designates an authentic GFP band (0.5 pg).

Comparative gel electrophoresis analysis of the 4H junction of U1 snRNA showed the junction adopted a coaxially stacked structure with almost perpendicular axes (Fig. 7.3). This result was very recently confirmed crystallographically (Pomeranz-Krummel et al., 2009). Perhaps the most extensively studied 4H junction in RNA is that of the hairpin ribozyme,... 

Figure 15.1 General scheme showing the steps to be followed for the preparation of cytosolic, mitochondrial, and membrane brain proteins and for the enrichment of the cytosolic proteins prior to the 2-D gel electrophoresis analysis.

Piceno, Y. M., Noble, P. A., and Lovell, C. R. (1999). Spatial and temporal assessment of diazotroph assemblage composition in vegetated salt marsh sediments using denaturing gradient gel electrophoresis analysis. Microb. Ecol. 38, 157—167. 

Fig. 4. SDS-PAGE of FPLC purified MAbe. SDS mini-gel electrophoresis analysis of an FPLC-purified mouse MAb stained with Coomassie blue R. Track 1 shows standard mol-wt markers (for details see Fig. 2). The remaining tracks show different loadings of the same MAb. Characteristic heavy chains (60,000) and light chains (22,000) are clearly seen to be free of contamination by other proteins.

Stavreva, D.A., Ptacek, O., Plewa, M.J. and Gichner, T. (1998) Single cell gel electrophoresis analysis of genomic damage induced by ethyl methanesulfonate in cultured tobacco cells. Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis, 422, 323-330. 

The observation of at least two transitions is likely not due to the presence of a protein contaminant Our gel electrophoresis analysis of sodium dodecyl sulfate-treated YADH yielded only one band that corresponded to the molecular weight of a YADH subunit (10), Thus, the presence of labile species or domain(s) in the sample must account for the two transitions. For example, the low Tm transition could be attributed to the denaturation of a labile dissociated subunit or a labile domain in the tetramer. Such labile subunits or domains may be akin to the conformationally drifted species found for other dehydrogenases (2,5). The high Tm transition, in turn, may be attributable to the denaturation of an active tetramer, or coenzyme binding domain, because the transition exhibited the greatest response to NAD. Other alternatives are that tetrameric YADH reversibly dissociates and the subunits are responsible for the low Tm transition, or that the low and high Tm transitions can be attributed to thermally-induced dissociation and denaturation of the subunits, respectively. To aid the interpretation of the scans, additional DSC experiments were performed. 

PEG-PAsp(DPT) was then applied to construct a nanocarrier of short interference RNA (siRNA), with the ability to show effective RNA interference (RNAi) properties [115]. RNA is extremely unstable against nuclease attack, and thus the establishment of an efficient delivery system is crucial for promoting the RNAi therapy. The complexation behavior of PEG-PAsp(DPT) with siRNA was examined through gel electrophoresis and EtBr exclusion assay to confirm the formation of stable complexes. The free siRNA disappeared at the N/P ratio > 2 in a gel electrophoresis analysis, which was consistent with the result of the EtBr assay where a substantial fluorescence quenching of EtBr was observed at N/P > 2. 

Terashima, I., Suzuki, N., and Shibutani, S. (2002). 32P-Postlabeling/polyacrylamide gel electrophoresis analysis Application to the detection of DNA adducts. Chem Res Toxicol 15, 305-311. 

Fig. 2a shows the ECL detection results of both healthy and infected samples. From this figure we can see that, the ECL intensity of infected samples and uninfected samples has such a striking contrast that we can clearly distinguish them. In order to verify the feasibility of this method, 1% agarose gel electrophoresis analysis for PCR products was performed in the experiment (Fig. 2b). The electrophoresis condition is 1 % agarose gel at 80V for an hour. Lane 1 and lane 2 are all the PCR products of infected samples. Lane M represent markers (100 bp, 200 bp, 300 bp, 400 bp, 500 bp, 600 bp, 700 bp, 800 bp, 900 bp, 1000 bp). Lane 1-2 has a band between 400 and 500bp which was consistent with the expected PCR product of size...

Fig. 2. ECL detection results of both healthy and infected samples and the agarose gel electrophoresis analysis results of the PCR products.

Skynner, H. A., Rosahl, T. W., Knowles, M. R., Salim, K., Reid, L., Cothiliff, R., McAllister, G., and Guest, P. C. (2002) Alterations of stress related proteins in genetically altered mice revealed by two-dimensional in-gel electrophoresis analysis. Proteomics 2, 1018-25. 

Figure 4. DIGE (differential gel electrophoresis) analysis. A flow diagram illustrating the use of Cy3, CyS and Cy2 dyes in the analysis of control versus diseased samples. The Cy3 dye is used to label one protein sample (e.g. control sample), whilst the other is labeled with CyS (e.g. diseased/experimental sample). The labeling reaction is terminated and equal amounts of each labeled sample are combined. In parallel, equal concentrations of both control and diseased samples are pooled in one tube and labeled with Cy2. This labeled sample is used for normalisation purposes and acts as an internal standard. Both the mixture of Cy3 and CyS labeled proteins and the Cy2 labeled pooled sample are separated on the same gel. Each 2DE protein profile associated with each individual dye is visualized at a specific wavelength.

Tissot, J.D., Schifferli, J.A., Hochstrasser, D.F., Pasquali, C., Spertini, F., Clement, F., Fmtiger, S., Paquet, N., Hughes, G.J., and Schneider, P., 1994b, Two-dimensional polyacrylamide gel electrophoresis analysis of cryoglobulins and identification of an IgM-associated peptide. J. Immunol Methods 173 63-75. 

FIG. 2 Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of pork and chicken myofibrillar proteins treated with purified actinidin at various pH values. MHC, myosin heavy chain A, actin. Reprinted with permission from Nishiyama (2001, Figs. 2 and 5A). 

Zoetendal EG, Akkermans AD, De Vos WM. Temperature gradient gel electrophoresis analysis of 16S rRNA from human fecal samples reveals stable and host-specific communities of active bacteria. Appl Environ Microbiol. 1998 64 3854-3859. 

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