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Partial Characterization of Lactobacillus lactis Cell Envelope Proteins

Swiss Federal Dairy Research Institute, CH - 3097 Liebefeld-Berne, Switzerland

ABSTRACT

Proteins from both cell wall and cytoplasmic membrane of Lactobacillus lactis were investigated by sodium dodecyl sulfate electrophoresis, isoelectric focusing, and a combined bidimensional procedure. A clear distinction between peptide profiles of cell wall and cytoplasmic membrane was obtained. Proteins were a heterogeneous collection. Polyacrylamide slab gels resolved proteins with molecular weights between 10,000 and 200,000 with a predominance of low molecular weight species. Treatment of whole cells with different detergents led to a selective release of cell proteins. Amino acid analysis of cell wall proteins solubilized by extraction into sodium dodecyl sulfate provided convincing evidence of the ambivalent character of the proteins. Relatively large amounts and numbers of proteins with a wide molecular weight spectrum could be released only by addition of a chelating agent in a low ionic strength-solution at neutral pH.