Alteration in the electrophoretic mobility of OmpC due to variations in the ammonium persulfate concentration in sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
Studies on Salmonella typhi and Salmonella typhimurium outer membrane proteins have shown that the relative position of OmpC porin in sodium dodecyl sulfate.polyacrylamide gel electrophoresis undergoes an important shift when the concentration of ammonium persulfate in the running gel is increased from 6 to 12 mM. The apparent molecular mass at these concentrations was estimated to be 34 and 40 kDa, respectively. Under similar electrophoretic conditions the apparent molecular mass estimated for OmpF was 37.6 and 38.2 kDa. Therefore, OmpC moves from a leading position to a position behind OmpF. For Escherichia coli OmpC the shift observed is less pronounced than that occurring in Salmonellae.
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Departamento de Bioquímia y Biología Molecular, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago.
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D000645:Ammonium Sulfate; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000032:analysis; D008970:Molecular Weight; D018272:Porins; D012485:Salmonella typhi / Q000032:analysis; D012486:Salmonella typhimurium / Q000032:analysis; D012967:Sodium Dodecyl Sulfate
D001425:Bacterial Outer Membrane Proteins; D018272:Porins; C031276:ammonium peroxydisulfate; D012967:Sodium Dodecyl Sulfate; D000645:Ammonium Sulfate