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| pubmed-article:1900281 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:1900281 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:1900281 | lifeskim:mentions | umls-concept:C0031437 | lld:lifeskim |
| pubmed-article:1900281 | lifeskim:mentions | umls-concept:C0162326 | lld:lifeskim |
| pubmed-article:1900281 | lifeskim:mentions | umls-concept:C1136254 | lld:lifeskim |
| pubmed-article:1900281 | lifeskim:mentions | umls-concept:C0125178 | lld:lifeskim |
| pubmed-article:1900281 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:1900281 | pubmed:dateCreated | 1991-4-8 | lld:pubmed |
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| pubmed-article:1900281 | pubmed:abstractText | Lactacin F is a heat-stable bacteriocin produced by Lactobacillus acidophilus 11088. A 63-mer oligonucleotide probe deduced from the N-terminal lactacin F amino acid sequence was used to clone the putative laf structural gene from plasmid DNA of a lactacin F-producing transconjugant, L. acidophilus T143. One clone, NCK360, harbored a recombinant plasmid, pTRK160, which contained a 2.2-kb EcoRI fragment of the size expected from hybridization experiments. An Escherichia coli-L. acidophilus shuttle vector was constructed, and a subclone (pTRK162) containing the 2.2-kb EcoRI fragment was introduced by electroporation into two lactacin F-negative strains, L. acidophilus 89 and 88-C. Lactobacillus transformants containing pTRK162 expressed lactacin F activity and immunity. Bacteriocin produced by the transformants exhibited an inhibitory spectrum and heat stability identical to those of the wild-type bacteriocin. An 873-bp region of the 2.2-kb fragment was sequenced by using a 20-mer degenerate lactacin F-specific primer to initiate sequencing from within the lactacin F structural gene. Analysis of the resulting sequence identified an open reading frame which could encode a protein of 75 amino acids. The 25 N-terminal amino acids for lactacin F were identified within the open reading frame along with an N-terminal extension, possibly a signal sequence. The lactacin F N-terminal sequence, through the remainder of the open reading frame (57 amino acids; 6.3 kDa), correlated extremely well with composition analyses of purified lactacin F which also predicted a size of 51 to 56 amino acid residues. Molecular characterization of lactacin F identified a small hydrophobic peptide that may be representative of a common bacteriocin class in lactic acid bacteria. | lld:pubmed |
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| pubmed-article:1900281 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1900281 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1900281 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1900281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1900281 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1900281 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:1900281 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:1900281 | pubmed:author | pubmed-author:KlaenhammerT... | lld:pubmed |
| pubmed-article:1900281 | pubmed:author | pubmed-author:MurianaP MPM | lld:pubmed |
| pubmed-article:1900281 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1900281 | pubmed:volume | 173 | lld:pubmed |
| pubmed-article:1900281 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1900281 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1900281 | pubmed:pagination | 1779-88 | lld:pubmed |
| pubmed-article:1900281 | pubmed:dateRevised | 2010-9-9 | lld:pubmed |
| pubmed-article:1900281 | pubmed:meshHeading | pubmed-meshheading:1900281-... | lld:pubmed |
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| pubmed-article:1900281 | pubmed:meshHeading | pubmed-meshheading:1900281-... | lld:pubmed |
| pubmed-article:1900281 | pubmed:meshHeading | pubmed-meshheading:1900281-... | lld:pubmed |
| pubmed-article:1900281 | pubmed:meshHeading | pubmed-meshheading:1900281-... | lld:pubmed |
| pubmed-article:1900281 | pubmed:meshHeading | pubmed-meshheading:1900281-... | lld:pubmed |
| pubmed-article:1900281 | pubmed:meshHeading | pubmed-meshheading:1900281-... | lld:pubmed |
| pubmed-article:1900281 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1900281 | pubmed:articleTitle | Cloning, phenotypic expression, and DNA sequence of the gene for lactacin F, an antimicrobial peptide produced by Lactobacillus spp. | lld:pubmed |
| pubmed-article:1900281 | pubmed:affiliation | Department of Food Science, North Carolina State University, Raleigh 27695-7624. | lld:pubmed |
| pubmed-article:1900281 | pubmed:publicationType | Journal Article | lld:pubmed |
