Sodium dodecyl sulfate , gel

Guttman, A, On the Separation Mechanism of Capillary Sodium Dodecyl Sulfate-Gel Electrophoresis of Proteins, Electrophoresis 16, 611, 1995. 

Guttman, A., Shieh, P, Lindahl, J., and Cooke, N., Capillary sodium dodecyl sulfate gel electrophoresis of proteins. II. On the Ferguson method of polyethylene oxide gels, /. Chromatogr., 676, 227, 1994. 

Guttman, A. and Nolan, J., Comparison of the separation of proteins by sodium dodecyl sulfate-slab gel electrophoresis and capillary sodium dodecyl sulfate-gel electrophoresis, Anal. Biochem., 221, 285, 1994. 

A. Gerstner, Z. Csapo, M. Sasvari-Szekely, and A. Guttman, Ultrathin sodium dodecyl sulfate gel electrophoresis of proteins Effect of gel composition and temperature on the separation of sodium dodecyl sulfate-protein complexes, Electrophoresis, 21, 834 (2000). 

The easiest way to detect a protein modification seems to be the mass measurement of all peptides generated by enzymatic digestion. The comparison with the predicted peptide masses from the sequence of the protein identifies unmodified peptides and unexplained masses would give indications to modified peptides. Unfortunately, this is not a suitable approach in practice. In many peptide mapping experiments done with the MALDI mass mapping technique, up to 30% of the measured masses remain unexplained. This is probably due to protein contaminations from human keratins, chemical modifications introduced by gel electrophoresis and the digestion procedure, and other proteins present at low levels in the piece excised from the sodium dodecyl sulfate gel. The detection of a protein modification requires a more specific analysis. 

Hu, D. H., Kimura, S., and Maruyama, K. (1986). Sodium dodecyl sulfate gel electrophoresis studies of connectin-like high molecular weight proteins of various types of vertebrate and invertebrate muscles./. Biochem. (Tokyo) 99, 1485—1492. 

Creatine kinase was purified from rabbit muscle by the method of Kuby et al, (4). Rabbit muscle pyruvate kinase was purchased from Boehringer. Porcine muscle adenylate kinase was purchased from Sigma, and was further purified by gel filtration on Sephadex G-50. The enzymes were homogeneous as judged by their specific activities and by their migration as single components in sodium dodecyl sulfate gel electrophoresis. Proton NMR spectra at 250 MHz of 0.5-2.0 mM enzyme sites in 0 solution were obtained with a Bruker WM 250 MHz pulse FT spectrometer at 25°. At least 256 transients were accumulated over 8192 data points using 16 bit A/D conversion. Relaxation rates and histidine pK values were determined by standard NMR methods (5, 6),... 

Li, Y., Buch, J.S., Rosenberger, F., DeVoe, D.L., Lee, C.S., Integration of isoelectric focusing with parallel sodium dodecyl sulfate gel electrophoresis for multidimensional protein separations in a plastic microfluidic network. Anal. Chem. 2004, 76, 742-748. 

Fig. 27.—A and B Electrophoresis and agar diffusion of isoantibodies in gels 4 and 10 (of Fig. 26B). C Sodium dodecyl sulfate gel-electrophoretic patterns for the anti-lactose isoantibodies (Ab), light (L) and heavy (H) chains and dissociated isoantibodies (gels 6, 7, 8, 9, and 10 of Fig. 26B). (Reprinted with permission from Journal of Protein Chemistry, Volume 6, J. H. Pazur, M. E. Tay, B. A. Pazur, and F. J. Miskiel, pp. 387-399, copyright 1987 Journal of Protein Chemistry.)...

Improved silver staining procedure for fast staining in PhastSystem Development Unit. 1. Staining of sodium dodecyl sulfate gels. Electrophoresis 9,... 

Vol. L [5]. Direct Identification of Specific Glycoproteins, Antigens in Sodium Dodecyl Sulfate Gels. K. Burridge. 

Guttman A (1996). Capillary sodium dodecyl sulfate-gel electrophoresis of proteins. Electrophoresis. 17 1333-1341. 

Sotelo, C.G., Pineiro, C., Perez-Martin, R.I., and Gallardo, J.M. 2000. Analysis of fish and squid myofibrillar proteins by capillary sodium dodecyl sulfate gel electrophoresis Actin and myosin quantification. Ear. Food Res. Technol. 211, 443-448. 

Moeremans, M., et al. (1986). Ferri-dye Collodial Iron Binding Followed by Peris Reaction for the Staining of Proteins Transferred from Sodium Dodecyl Sulfate Gels to Nitrocellulose and Positively Charged Nylon Membranes, /Ina/. biochem. 153 18-22. 

Maruyama, K., et al. (1984). Detection of Calcium Binding Proteins by Ca Autoradiography on Nitrocellulose Membrane After Sodium Dodecyl Sulfate Gel Electrophoresis, J. Biochem. 95 511-519. 

Maruyama, K., Mikawa, T., and Ebashi, S. (1984) Detection of calcium binding proteins by Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis./. Biochem. 95, 511-519. 

Generally, purification is measured by determining the enzyme specific gravity using a spectrophotometer, sodium dodecyl sulfate gel electrophoresis, isoelectric focusing, and a mass spectrophotometer. 

Blue staining profile of membrane proteins separated by sodium dodecyl sulfate gel electrophoresis. 

Fig. 2. Distribution of radioactivity covalently attached to (Na + K ) adenosine triphosphatase that has been photolyzed in the presence of [ ClCM-cymarin. Samples of enzyme that had been photolyzed either in the presence of the complete MgATP phosphorylating system (O) or the complete system plus a 25-fold excess of cymarin as protector ( ) were run on sodium dodecyl sulfate gels which were scanned, sliced, and counted. The A2M trace from the gel with the unprotected sample was divided into segments exactly as the gel had been sliced. The mean of each of these segments was calculated, and the values were plotted ( ). The units of are arbitrary since the scanner was uncalibrated. The three protein components are (a) cross-linked /3 dimer (b) large chain (c) small chain.

Sodium phosphate, monobasic monohydrate, sodium phosphate dibasic heptahydrate + sodium dodecyl sulfate (Gel buffer)... 

Pre-cast 4-20 % gradient gels for sodium dodecyl sulfate gel electrophoresis (SDS-PAGE) (e.g., Tris-glycine gels). 

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