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Abstract
<p class="first" id="d9084266e61">A discontinuous sodium dodecyl sulfate-polyacrylamide
gel electrophoresis (SDS-PAGE)
system for the separation of proteins in the range from 1 to 100 kDa is described.
Tricine, used as the trailing ion, allows a resolution of small proteins at lower
acrylamide concentrations than in glycine-SDS-PAGE systems. A superior resolution
of proteins, especially in the range between 5 and 20 kDa, is achieved without the
necessity to use urea. Proteins above 30 kDa are already destacked within the sample
gel. Thus a smooth passage of these proteins from sample to separating gel is warranted
and overloading effects are reduced. This is of special importance when large amounts
of protein are to be loaded onto preparative gels. The omission of glycine and urea
prevents disturbances which might occur in the course of subsequent amino acid sequencing.
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