Abstract

The behaviors of all the components of glycine and tricine sodium dodecyl sulfate-polyacrylamide gel electrophoresis system in the course of separation of polypeptide-dodecyl sulfate complexes are investigated by computer simulation. In both of the systems, the leading chloride ion zone is followed by concentrated dodecyl sulfate zone, the length of which gradually increases with the time of electrophoresis. Under the postulated conditions and the values of physico-chemical parameters of the components of the systems, almost all the polypeptides migrate as the dodecyl sulfate-polypeptide complexes. These complexes are stacked between the dodecyl sulfate zone and the terminating glycine or tricine zone when they reach the separation gel. The high mobility complexes are not overtaken by the terminating glycine in the separation gel but stacked between the dodecyl sulfate and the glycine zone, while, all the complexes are overtaken in the separation gel by the terminating tricine and separated in the separation gel. Thus, the reason for the usefulness of tricine for the separation of the low molecular complexes is clarified by the computer simulation.

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