Cell surface protein of Salmonella typhimurium

Lactoperoxidase-catalyzed radioiodination with Na125I was performed both on intact Salmonella typhimurium 1195 and on ghost membrane isolated from the same bacterial strain. Ghost membrane was also prepared from radioiodinated whole bacteria. The labelled proteins from both these ghost membrane preparations were compared by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate to identify the cell surface proteinmfrom the results obtained it was concluded that one major protein with an apparent molecular weight of 1200-1300 was exposed on the exterior surface of the ghost membrane.