Results 251 to 260 of about 920,072 (304)

Separation of Colicins by Polyacrylamide Gel Electrophoresis

Journal of Applied Bacteriology, 1972
S ummary : Colicins can be separated by polyacrylamide gel electrophoresis, so allowing multiple colicinogeny to be detected with a universal indicator strain.
K G, Hardy, H C, Neimark
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‘Laterally aggregated’ polyacrylamide gels for electrophoresis

ELECTROPHORESIS, 1992
AbstractA new method is described for producing highly porous polyacrylamide matrices: polymerization in presence of a preformed hydrophilic polymer. If a standard mixture of monomers (e.g., 5%T, 4%C) is polymerized in presence of, e.g., polyethylene glycol (PEG) 10 kDa, lateral chain aggregation occurs, with formation of large pore sizes.
P G, Righetti, S, Caglio, M, Saracchi, S, Quaroni   +3 more
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Micro-Electrophoresis on Polyacrylamide Gels

1973
Polyacrylamide gels were introduced in 1959 by Raymond and Weintraub, as supports for electrophoretic separations. The polyacrylamide gel is produced by polymerising acrylamide, with N,N-methylenebisacrylamide or ethylene diacrylate as the cross-linking component. Catalytic redox systems, which yield free radicals, are used to initate copolymerisation (
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SDS – polyacrylamide gel electrophoresis of lipopolysaccharides

Canadian Journal of Microbiology, 1975
Lipopolysaccharides (LPS) prepared from four different species of Neisseria have been separated by SDS – polyacrylamide gel electrophoresis. Each LPS possessed a characteristic mobility on gels. Examination of the effect of acrylamide concentration on migration illustrated that the basis of the separation was molecular size, and not intrinsic charge.
R R, Russell, K G, Johnson
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SDS Polyacrylamide Gel Electrophoresis of Proteins

2003
Probably the most widely used of techniques for analyzing mixtures of proteins is SDS polyacrylamide gel electrophoresis. In this technique, proteins are reacted with the anionic detergent, sodium dodecylsulfate (SDS, or sodium lauryl sulfate) to form negatively charged complexes.
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A miniaturized system for electrophoresis on polyacrylamide gels

Analytical Biochemistry, 1979
The design, construction, and use of a simple economical system for gel electrophoresis are described, along with effective procedures and the required materials. Examples of successful use of the system are presented.
Z I, Ogita, C L, Markert
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Polyacrylamide Gel Electrophoresis of Lysates of Mycoplasmas

Research in Veterinary Science, 1970
The technique of Razin & Rottem (1967) for electrophoretic comparison of mycoplasmas has been modified, principally by carrying out the electrophoresis on flat gel slabs, and has been used to examine lysates of several mycoplasma preparations. The 6 different species compared could readily be distinguished, while different batches and isolates of the ...
H, Zola, W, Baxendale, L J, Sayer
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Fractionation of oligodeoxynucleotides by polyacrylamide gel electrophoresis

Analytical Biochemistry, 1969
Abstract Polyacrylamide gel electrophoresis has been used to fractionate mixtures of oligomers produced by enzymic digestion of dAT copolymer with pancreatic DNase I. Fractions with degrees of polymerization from about 6 to beyond 40 were obtained with high resolution.
E, Elson, T M, Jovin
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Discontinuous polyacrylamide gel electrophoresis of RNA

Analytical Biochemistry, 1972
Abstract A discontinuous polyacrylamide gel system is described which allows the simultaneous resolution of 38S, 28S, 18S, 5S, and 4S RNA molecules from total RNA extracts on a single gel. The gels can be constructed easily and reproducibly without special apparatus. Also reported is the use of an octadecene solution to facilitate overlayering of low
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Gradient SDS Polyacrylamide Gel Electrophoresis

2003
The preparation of fixed-concentration polyacrylamide gels has been described in Chapter 6. However, the use of polyacrylamide gels that have a gradient of increasing acrylamide concentration (and hence decreasing pore size) can sometimes have advantages over fixed-concentration acrylamide gels. During electrophoresis in gradient gels, proteins migrate
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