Sodium dodecyl sulphate polyacrylamide gel

Sodium dodecyl sulphate polyacrylamide gel electrophoresis Single step isolation and identification procedure White rot fungi... 

Molecular masses of the same enzymes of different species are different. Molecular mass of the laccase of Pleorotus ostreatus was found to be 66.8 kDa by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) [48]. Purified enzyme of T. versicolor having a single band with a molecular mass of 68 kDa was in the same range with the molecular weights of laccase isoforms isolated from 2,5-xylidine-induced cultures of T. versicolor [49]. 

While studying the binding of mercury by chromatin of rats injected with mercuric chloride, the nonhistone chromatin proteins in rat and kidney cell nuclei were shown to be mainly responsible for the mercury deposition [43]. The mercury-binding nonhistone proteins were found to be heterogeneous by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. 

F5. Farrer, M., Game, F. L., Adams, P. C., Laker, M. F., and Alberti, K. G. M. M., A simple sensitive technique for classification of apolipoprotein(a) isoforms by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Clin. Chim. Acta 207, 215-225 (1992). 

Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) represents the most commonly used analytical technique in the assessment of final product purity (Figure 3.31). This technique is well established and easy to perform. It provides high-resolution separation of polypeptides on the basis of their molecular mass. Bands containing as little as 100 ng protein can be visualized by staining the gel with dyes such as Coomassie blue. Subsequent gel analysis by scanning laser densitometry allows quantitative determination of the protein content of each band (thus allowing quantification of protein impurities in the product). 

Chemical purity. The purity of the protein product is analysed in comparison with a reference preparation by a suitable method, such as liquid chromatography, capillary electrophoresis or sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). 

Takazawa, K. Passareiro, H. Dumont, J.E. Erneux, C. Purification of bovine brain inositol 1,4,5-trisphosphate 3-kinase. Identification of the enzyme by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Biochem. J., 261, 483-488 (1989)... 

Szewczyk, B. and Kozloff, L. M. (1985) A method for the efficient blotting of strongly basic proteins from sodium dodecyl sulphate-polyacrylamide gels to nitrocellulose. Anal. Biochem. 50,403-407. 

SDS-PACE, sodium dodecyl sulphate-polyacrylamide gel electrophoresis. 

SDS-PAGE, sodium dodecyl sulphate-polyacrylamide gel electrophoresis HPLC, high performance liquid chromatography PCR, polymerase chain reaction IEF, isoelectric focusing HPSEC, high performance size-exclusion chromatography DNA, DNA-binding fluorochrome CPE, cytopathic effect Had, hemadsorption PMA, production of murine antibodies. 

PL PVC Q RPC S SM SP SDS SDS-PAGE TEAE TAM Ve V0 vs Vt X y reversible complex ptotein-ligand poly vinyl chloride quaternary amine reverse phase chromatography Sulfonate Sulfomethyl Sulfopropyl sodium dodecyl sulphate sodium dodecyl sulphate - polyacrylamide gel electrophoresis Triethylaminoethyl Trimethylaminomethyl elution volume interstitial volume of the porous matrix total solvent volume within the pores total column volume solute concentration in the original solution solute concentration in the extract... 

Tsuji, K. (1991). High performance capillary electrophoresis of proteins. Sodium dodecyl sulphate-polyacrylamide gel-filled capillary column for the determination of recombinant biotechnology-derived proteins. J. Chromatogr. 550, 823-830. 

Schagger, H., von Jagow, G. (1987). Tridne-sodium dodecyl sulphate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 KDa. Anal. Biochem., 79, 544-552. 

Burnette, W. N. (1981) Western blotdng Electrophoredc transfer of proteins from sodium dodecyl sulphate-polyacrylamide gels to unmodihed nitrocellulose and radiographic detecdon with antibody and radioiodinated protein A. Anal Biochem. 112,195-203. 

One of the most interesting problems concerning the cytochrome P-450 system has been its multiplicity, for it is difficult to conceive of a single enzyme system having the ability to oxidise in a specific way such a wide variety of substrates. Current data suggest that there are at least three forms of the enzymes present in rat liver microsomes. Optical spectra reveal two forms of the CO-bound reduced cytochrome P-450, one with a maximum at 448 nm (such as is induced by 3-methylcholanthrene) and one at 450 nm (as is induced by phenobarbital), and SDS (sodium dodecyl sulphate) polyacrylamide gel electrophoresis shows three peaks corresponding to molecular weights of 44000 (phenobarbital), 50000, and 53000 (3-methylcholanthrene) [117]. Differences are also seen in the ESR spectra of P-450 in rat liver microsomes induced by different chemicals and there are further differences when... 

The quality control of immunoglobulins includes potency tests and conventional tests for safety and sterility. The potency tests consist of toxin or virus neutralization tests that parallel those used for the potency assay of immune sera, except that for in-process control of some immunoglobulins wider use is made of in vitro assays. In addition to the safety and sterility tests, total protein is determined by nitrogen estimations, the protein composition by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and molecular size by high performance liquid chromatography. The presence of immunoglobulins derived from species other than humans is excluded by precipitin tests. Table 23.4... 

Rat insulinoma tumour cell line m5F Sodium dodecyl sulphate-polyacrylamide gel electrophoresis Elimination half-life... 

Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE)... 

All the above studies were carried out with preparations purified only 2-7-fold with respect to cytochrome P-450. In recent work by Atsuta and Okuda, up to 22-fold purification was reported [139]. The preparation was not homogenous as judged from sodium dodecyl sulphate polyacrylamide gel electrophoresis. It was shown by thermal inactivation as well as use of different inhibitors and activators that the same enzyme is involved in the 26-hydroxylation of 5 -cholestane-3a,7 -diol and 5j8-cholestane-3a,7a,12a-triol. 

Burnette, W. W. (1980). Western blotting Electrophoretic transfer of the proteins from sodium dodecyl sulphate polyacrylamide gels to unmodified niirocellulo.se and radigraphie detection with antibody and radioiodinaied protein A. Anal. Siochem, 112, 195-203. 

Bruce, K.D. and Pennington, T.H. 1991, Clonal analysis of non-typahle Haemophilus influenzae hy sodium dodecyl sulphate-polyacrylamide gel electrophoresis of whole cell polypeptides. J Med Microbiol 34 277-283. 

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