Purification and Partial Characterization of a Bacteriocin from
            <i>Serratia marcescens</i>

Foulds, John

doi:10.1128/jb.110.3.1001-1009.1972

Cited by 47 publications

(21 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Production of bacteriocin was per cell increased with the aeration of the culture grown on the shaker not due to increase in cell number ( Table 2). The biological activity of partially purified bacteriocin was rapidly destroyed and inactivated by proteolytic enzymes (trypsin and chyrnotrypsin) proving that this bacteriocin is a simple protein and that is in agreement with the report of Foulds (1972).…”

Section: Discussionsupporting

confidence: 90%

“…Bacteriocins are reported to be mostly simple protein in nature and exhibit a remarkable degree of specificity. Susceptibility to a given bacteriocin is usually restricted to bacterial species which carry a specific receptor on the cell envelope ; thus, each bacteriocin has a specificity of attachment and a specific mode of action and these specifics are independent (Nomura 1967;Foulds 1972).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Partial purification and characterization of bacteriocin from Yersinia kristensenii

Toora¹

1995

Journal of Applied Bacteriology

View full text Add to dashboard Cite

A raw milk bacterial isolate, identified as Yersinia kristensenii was found to produce a bacteriocin which was inhibitory to Yersinia enterocolitica but not to other selected species of Yersinia or Gram-negative bacteria. Maximum production of bacteriocin was obtained when the organism was grown in shake culture at 28 degrees C. Mitomycin C at a concentration of 0.5 micrograms ml-1 induced bacteriocin production. The bacteriocin was partially purified and characterized by ammonium sulphate fractionation and gel filtration. The bacteriocin was completely inactivated when treated with proteolytic enzymes (trypsin and chymotrypsin). Bacteriocin activity was heat-resistant and it retained some of its activity after 5 min at boiling temperature. A total of 15 bacteriocin sensitive-suspected food isolates were further identified biochemically as Yersinia enterocolitica and a non-sensitive isolate was identified as Yersinia intermedia.

show abstract

Section: Discussionsupporting

confidence: 90%

Section: Introductionmentioning

confidence: 99%

Partial purification and characterization of bacteriocin from Yersinia kristensenii

Toora¹

1995

Journal of Applied Bacteriology

View full text Add to dashboard Cite

show abstract

“…Efficiency of conjugation and sensitivity to colicin L were measured by standard procedures exactly as described previously (14). A crude colicin preparation (NaCl extract) was obtained as described by Foulds (19). Envelope prepartion and sodim dodeyl sufatepolyacrylande gel electrophoresis.…”

Section: Materias and Methods Bacteria Phages And Microbiological Tmentioning

confidence: 99%

Apparent bacteriophage-binding region of an Escherichia coli K-12 outer membrane protein

Cole¹,

Chen-Schmeisser²,

Hindennach³

et al. 1983

J Bacteriol

View full text Add to dashboard Cite

The 325-residue OmpA protein is one of the major outer membrane proteins of Escherichia coli. It serves as the receptor for several T-even-like phages and is required for the action of certain colicins and for the stabilization of mating aggregates in conjugation. We have isolated two mutant alleles of the cloned ompA gene which produce a protein that no longer functions as a phage receptor. Bacteria possessing the mutant proteins were unable to bind the phages, either reversibly or irreversibly. However, both proteins still functioned in conjugation, and one of them conferred colicin L sensitivity. DNA sequence analysis showed that the phage-resistant, colicin-sensitive phenotype exhibited by one mutant was due to the amino acid substitution Gly --Arg at position 70. The second mutant,

show abstract

“…Serratia marcescens strain JF246 produces a bacteriocin (8) that is apparently closely related to colicin L produced by Escherichia coli strain 398. Antibody prepared against pure bacteriocin JF246 inactivated colicin L-398.…”

mentioning

confidence: 99%

TolF locus in Escherichia coli: chromosomal location and relationship to loci cmlB and tolD

Foulds¹

1976

J Bacteriol

View full text Add to dashboard Cite

The tentative map position on the Escherichia coli chromosome of the tolF locus, determining tolerance to colicins A, E2, E3, K, and L, has been confirmed by three-point transduction. It lies between the aroA and pyrD loci at about 21 min on the linkage map of Bachmann et al. (1976). The cmlB locus, determining increased resistance to the antibiotics chloramphenicol and tetracycline, also lies in this region (Reeve, 1966). Phenotypic and genetic comparison of isogenic strains that carry a mutation in either the tolF or cmlB locus makes it likely that these loci are closely related or identical. The tolD locus determining tolerance to colicins E2 and E3 as well as increased resistance to antibiotics has been reported to be located close to the aroA locus as a result of conjugation experiments (Eriksson-Grennberg et al. 1965). However, tolD did not cotransduce with any of several loci in this region, indicating that the mutation is not located within the region of the genetic map corresponding to approximately 19 to 22.5 min.

show abstract

Purification and Partial Characterization of a Bacteriocin from Serratia marcescens

Cited by 47 publications

References 26 publications

Partial purification and characterization of bacteriocin from Yersinia kristensenii

Partial purification and characterization of bacteriocin from Yersinia kristensenii

Apparent bacteriophage-binding region of an Escherichia coli K-12 outer membrane protein

TolF locus in Escherichia coli: chromosomal location and relationship to loci cmlB and tolD

Contact Info

Product

Resources

About