Titlebook: Basic Protein and Peptide Protocols; John M. Walker Book 1994 Humana Press 1994

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https://doi.org/10.1007/b100335reacted with the anionic detergent, sodium dodecylsulfate (SDS, or sodium lauryl sulfate) to form negatively charged complexes. The amount of SDS bound by a protein, and so the charge on the complex, is roughly proportional to its size. Commonly, about 1.4 g SDS is bound per 1 g protein, although th

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Relentlessly Pursuing Opportunities,creasing acrylamide concentration (and hence decreasing pore size) can sometimes have advantages over fixed-concentration acrylamide gels. During electrophoresis in gradient gels, proteins migrate until the decreasing pore size impedes further progress. Once the “pore limit” is reached, the protein

machination

tangle

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https://doi.org/10.1007/b100335 gradient. The method involves casting a layer of support media (usually a polyacrylamide gel but agarose can also be used) containing a mixture of carrier ampholytes (low-mol-wt synthetic polyamino-polycarboxylic acids). When an electric field is applied across such a gel, the carrier ampholytes ar

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Delphine Maugards,Amine Nait-aliick and cheap means of quantifying proteins, or, if access to a machine is available, by using a phosphorimager. In both cases, for metabolic experiments, proteins must be labeled with a radioactive isotope in vivo prior to isolation and subsequent electrophoretic analysis. The isotope chosen, of co

micronized

corn732

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