The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N ‐terminal region of bovine lactoferrin
Abstract
A physiologically diverse range of Gram‐positive and Gram‐negative bacteria was found to be susceptible to inhibition and inactivation by lactoferricin B, a peptide produced by gastric pepsin digestion of bovine lactoferrin. The list of susceptible organisms includes Escherichia coli, Salmonella enteritidis, Klebsiella pneumoniae, Proteus vulgaris, Yersinia enterocolitica, Pseudomonas aeruginosa, Campylobacter jejuni, Staphylococcus aureus, Streptococcus mutans, Corynebacterium diphtheriae, Listeria monocytogenes and Clostridium perfringens. Concentrations of lactoferricin B required to cause complete inhibition of growth varied within the range of 0.3 to 150 μg/ml, depending on the strain and the culture medium used. The peptide showed activity against E. coli O111 over the range of pH 5.5 to 7.5 and was most effective under slightly alkaline conditions. Its antibacterial effectiveness was reduced in the presence of Na + , K + , Mg 2+ or Ca 2+ ions, or in the presence of various buffer salts. Lactoferricin B was lethal, causing a rapid loss of colony‐forming capability in most of the species tested. Pseudomonas fluorescens, Enterococcus faecalis and Bifidobacterium bifidum strains were highly resistant to this peptide.
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Citations
Cites
The significance of iron in infection
Bullen, J. J. (1981) · Clinical Infectious Diseases · doi:10.1093/clinids/3.6.1127 · Cited by 603
Cited by
Lactoferrin: structure, function and applications
González-Chávez, S. A., Arévalo-Gallegos, S., & Rascón-Cruz, Q. (2009) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2008.07.020 · Cited by 759
Bioactive milk peptides: a prospectus.
Clare, D. A., & Swaisgood, H. E. (2000) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(00)74983-6 · Cited by 718
Lactoferrin a multiple bioactive protein: an overview
García-Montoya, I. A., Cendón, T. S., Arévalo-Gallegos, S., & Rascón-Cruz, Q. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.06.018 · Cited by 473
Harmsen, M. C., Swart, P. J., Bethune, M.-P. D., Pauwels, R., Clercq, E. D., The, T. B., & Meijer, D. K. F. (1995) · Journal of Infectious Diseases · doi:10.1093/infdis/172.2.380 · Cited by 379
Lactoferrin: a natural Glycoprotein involved in iron and inflammatory homeostasis
Rosa, L., Cutone, A., Lepanto, M., Paesano, R., & Valenti, P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091985 · Cited by 376
Metadata
- Authors
- Bellamy, W., Takase, M., Wakabayashi, H., Kawase, K., & Tomita, M.
- Venue
- Journal of Applied Bacteriology
- Publisher
- Wiley
- Published
- 1992-12
- Volume
- 73
- Issue
- 6
- Pages
- 472-479
- ISSN
- 0021-8847 (ISSN-L)
- OpenAlex
- W1997947168
- Cited by
- 588
- References
- 1
- FWCI
- 4.57
- Type
- journal article
- Language
- en
- Open access
- closed
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- Bellamy, W., Takase, M., Wakabayashi, H., Kawase, K., & Tomita, M. (1992). Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N ‐terminal region of bovine lactoferrin. Journal of Applied Bacteriology. https://doi.org/10.1111/j.1365-2672.1992.tb05007.x
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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