Immunological characterization of an Escherichia coli strain which is lacking cytochrome d.

AUTOR(ES)

Kranz, R G

RESUMO

The isolated membranes from an Escherichia coli mutant strain which lacks spectroscopically detectable levels of cytochromes d, a1, and b558 also have abnormally low levels of N,N,N',N'-tetramethyl-p-phenylenediamine oxidase activity. In this paper, it is shown that the material previously identified as the N,N,N',N'-tetramethyl-p-phenylenediamine oxidase is, in fact, the two-subunit cytochrome d complex. Antisera directed against the native cytochrome d complex as well as against each of two subunits apparent on sodium dodecyl sulfate-polyacrylamide gels were used to show that the mutant strain lacks both subunits of the cytochrome d complex. Introduction of F-prime F152 into the mutant strain restored the two subunits along with the spectroscopic and enzymatic activity associated with the cytochrome d complex.

Documentos Relacionados

• Isolation and characterization of an Escherichia coli mutant lacking cytochrome d terminal oxidase.
• Potentiometric analysis of the cytochromes of an Escherichia coli mutant strain lacking the cytochrome d terminal oxidase complex.
• Isolation and characterization of an Escherichia coli mutant lacking the cytochrome o terminal oxidase.
• Escherichia coli mutants with an altered sensitivity to cecropin D.
• AN IMMUNOLOGICAL STUDY OF MUTANTS OF ESCHERICHIA COLI LACKING THE ENZYME TRYPTOPHAN SYNTHETASE1