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Genetic and biochemical characterization of an Escherichia coli K-12 mutant with an altered outer membrane protein.
- Source :
-
Antonie van Leeuwenhoek [Antonie Van Leeuwenhoek] 1981; Vol. 47 (4), pp. 325-37. - Publication Year :
- 1981
-
Abstract
- The properties of an Escherichia coli K-12 mutant are described which seemingly produces a "new" major outer membrane protein with an apparent molecular weight of 40 000. This 40K protein was purified and its cyanogen bromide (CNBr) fragments were compared with those of several known major outer membrane proteins. A similarity was found between the CNBr fragments of the 40K protein and those of the OmpF protein (molecular weight 37 000). In addition, the 40K protein was found to be regulated exactly like the OmpF protein, and the mutation which causes the production of the 40K protein has been localized in (or very close to) the ompF gene. It is concluded that the 40K protein is a mutant form of the OmpF protein. The results provide additional evidence that the ompF gene at minute 21 is the structural gene for the OmpF protein.
- Subjects :
- Ampicillin metabolism
Bacterial Outer Membrane Proteins
Conjugation, Genetic
Culture Media
Cyanogen Bromide pharmacology
Electrophoresis, Polyacrylamide Gel
Escherichia coli analysis
Escherichia coli metabolism
Genes, Regulator
Membrane Proteins genetics
Molecular Weight
Transduction, Genetic
Escherichia coli genetics
Membrane Proteins analysis
Mutation
Subjects
Details
- Language :
- English
- ISSN :
- 0003-6072
- Volume :
- 47
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Antonie van Leeuwenhoek
- Publication Type :
- Academic Journal
- Accession number :
- 7044306
- Full Text :
- https://doi.org/10.1007/BF02350783