Purification of protein A, an outer membrane component missing in Escherichia coli K-12 ompA mutants.
Biochim Biophys Acta
; 493(1): 210-5, 1977 Jul 22.
Article
em En
| MEDLINE
| ID: mdl-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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01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Escherichia coli
/
Proteínas de Membrana
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1977
Tipo de documento:
Article