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  • Title: Purification of protein A, an outer membrane component missing in Escherichia coli K-12 ompA mutants.
    Author: Chai TJ, Foulds J.
    Journal: Biochim Biophys Acta; 1977 Jul 22; 493(1):210-5. PubMed ID: 328056.
    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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