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Some chemical and physical properties of nisin, a small-protein antibiotic produced by Lactococcus lactis.
  • W. Liu, J. N. Hansen
  • Chemistry, Medicine
  • Applied and environmental microbiology
  • 1 August 1990
Nisin is a small gene-encoded antimicrobial protein produced by Lactococcus lactis that contains unusual dehydroalanine and dehydrobutyrine residues. The reactivity of these residues towardExpand
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Identification and Characterization of the Structural and Transporter Genes for, and the Chemical and Biological Properties of, Sublancin 168, a Novel Lantibiotic Produced by Bacillus subtilis 168*
An antimicrobial peptide produced byBacillus subtilis 168 was isolated and characterized. It was named sublancin 168, and its behavior during Edman sequence analysis and its NMR spectrum suggestedExpand
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Structure, expression, and evolution of a gene encoding the precursor of nisin, a small protein antibiotic.
We have cloned and sequenced a gene (spaN) from Streptococcus lactis ATCC 11454 which encodes the peptide precursor of the small protein antibiotic nisin. The encoded precursor is 57 amino acidsExpand
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Identification and characterization of some bacterial membrane sulfhydryl groups which are targets of bacteriostatic and antibiotic action.
Covalent modification of sulfhydryl groups which become sensitive toward sulfhydryl agents during germination of Bacillus cereus spores exerts a profound bacteriostatic effect, resulting in outgrowthExpand
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Characterization of a chimeric proU operon in a subtilin-producing mutant of Bacillus subtilis 168.
The ability to respond to osmotic stress by osmoregulation is common to virtually all living cells. Gram-negative bacteria such as Escherichia coli and Salmonella typhimurium can achieveExpand
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Electrophoresis of ribonucleic acid on a polyacrylamide gel which contains disulfide cross-linkages.
  • J. N. Hansen
  • Chemistry, Medicine
  • Analytical biochemistry
  • 1 November 1976
Abstract A disulfide-containing analog of bis-acrylamide has been synthesized. When substituted for bis-acrylamide as the cross-linking agent in polyacrylamide-gel formation, a gel is formed whichExpand
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Enhancement of the chemical and antimicrobial properties of subtilin by site-directed mutagenesis.
Subtilin and nisin are gene-encoded antibiotic peptides that are ribosomally synthesized by Bacillus subtilis and Lactococcus lactis, respectively. Gene-encoded antibiotics are unique in that theirExpand
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Molecular cloning and sequencing of cDNAs encoding the proteolipid subunit of the vacuolar H(+)-ATPase from a higher plant.
To understand the molecular structure of the vacuolar H(+)-translocating ATPase from plants, cDNAs encoding the N,N'-dicyclohexylcarbodiimide-binding 16-kDa proteolipid from oat (Avena sativa L. var.Expand
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Structure and expression of a gene encoding the precursor of subtilin, a small protein antibiotic.
A gene has been cloned from Bacillus subtilis ATCC 6633 that encodes a 56-residue peptide precursor for the 32-residue peptide antibiotic, subtilin. The precursor contains serines, threonines, andExpand
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The antimicrobial effect of a structural variant of subtilin against outgrowing Bacillus cereus T spores and vegetative cells occurs by different mechanisms.
  • W. Liu, J. N. Hansen
  • Biology, Medicine
  • Applied and environmental microbiology
  • 1 February 1993
Subtilin is a ribosomally synthesized antimicrobial peptide that contains several unusual amino acids as a result of posttranslational modifications. Site-directed mutagenesis was employed toExpand
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