Apparent molecular weights of a heat-modifiable protein from the outer membrane of Escherichia coli in gels with different acrylamide concentrations.

The apparent molecular weights of the two forms of a heat-modifiable protein from the outer membrane of Escherichia coli K-12, estimated in gels with different concentrations of acrylamide, indicate that the protein binds excess amounts of sodium dodecyl sulfate, possibly due to large beta structures before boiling.