Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from Escherichia coli K-12.

Abstract

Major outer membrane proteins of Escherichia coli K-12 with apparent molecular weights ranging from 30,000 to 40,000 were resolved into four distinct bands by electrophoresis on an improved urea-sodium dodecyl sulfate (SDS)-polyacrylamide gel containing a high concentration of N,N'-methylenebisacrylamide. The electrophoretic mobilities of three of these… (More)

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