Protein gels electrophoretic analysis

Hiraoka, A., et al (1998). Sodium dodecyl sulfate-capillary gel electrophoretic analysis of molecular mass microheterogeneity of beta-trace protein in cerebrospinal fluid from patients with central nervous system diseases./. Chromatogr. A 802, 143-8. 

Barton et al. developed an assay enabling the study of the influence of DNA-binding proteins simply by gel electrophoretic analysis of oxidative G damage... 

B6. Becker, J., Higgins, G., and O Brien, J. R. P., Plasma proteins some chemical methods of fractionation starch gel electrophoretic analysis. Proc. Assoc. Clin. Biochem. 1, 83-84 (1961). 

Figure 10.17 Gel electrophoretic analysis of erythrocyte membrane proteins. 

Snyder, E.L., Dunn, B.E., Giometti, C.S., Napychank, P.A., Tandon, N.N., Ferri, P.M., and Hofmann, J.P., 1987, Protein changes occurring during storage of platelet concentrates. A two-dimensional gel electrophoretic analysis. Transfusion 27 335-341. 

Results of electrophoretic analysis of proteins in the allantoic fluid and blood serum before and after photodynamic treatment are presented in Figs. 5.5 and 5.6. Visually, we did not detect any changes in the position and intensity of protein bands. In order to quantitatively analyze these parameters we scanned the gels and measured the relative optical density of the bands (Figs. 5.7 and 5.8). 

Electrophoretic analysis is the most generally used method in the analysis of complex mixtures of proteins and the most widely employed supporting material is polyacrylamide gel (PAG), particularly in the presence of sodium dodecyl sulphate (SDS). 

Costas, M. 1992, Classification, identification and typing of bacteria by the analysis of their one-dimensional polyacrylamide gel electrophoretic protein patterns. Advances in Electrophoresis S 351-408. 

For proteomics analysis, all the proteins from a cell must be extracted and then separated from each other. Gel electrophoretic methods (section 3.2) are most powerful, especially two-dimensional gel electrophoresis (2D-GE), which is capable of separating thousands of proteins in a single run (section 3.2.5). 

Na-K ATPase is composed of two different subunits, one of about 100000 (a-subunit) and one of about 50000 (yS-subunit), as shown by sodium dodecyl-sulfate (SDS) gel electrophoresis [75,76]. Since both subunits are glycoproteins and therefore bind different amounts of SDS as compared to normal proteins, their SDS gel electrophoretic mobility, and hence their apparent molecular weights can deviate considerably. Recently the molecular weights of the separated subunits of Na-K ATPase from rabbit kidney outer medulla have been determined more accurately by sedimentation equilibrium analysis in the absence of detergents [77]. The value for the a-subunit thus determined is 131000 (120600 for its protein part) and 61 800 for the /8-subunit (42 800 for its protein part). 

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