Abstract
Outer membrane materials prepared from an Escherichia coli ompA (tolG) strain do not contain one of the major outer membrane proteins found in ompA + strains. This protein has been purified in high yield from detergent-solubilized cell envelope material prepared from an ompA + strain by preparative electrophoresis in polyacrylamide gels containing sodium dodecyl sulfate. The purified protein is homogeneous in three electrophoretic systems, contains 2 mol of reducing sugar/mol of peptide and has alanine as the N-terminal amino acid. The amino acid composition is nearly identical to outer membrane protein II∗ or B∗ purified by others from incompletely solubilized cell envelope material. Thus, the fraction of outer membrane protein II∗ or B∗ that is difficult to solubilize is identical with the more readily solubilized fraction.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Protein Structure
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