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pubmed-article:1368836pubmed:abstractTextAcidocin 8912, a bacteriocin produced by Lactobacillus acidophilus TK8912, was purified by ammonium sulfate fractionation and successive chromatographies on CM-cellulose, Sephadex G-50, Sephadex G-25, and reversed-phase HPLC on Aquapore RP-300. The purified acidocin 8912 migrated as a single band on SDS-PAGE. The molecular weight was estimated to be 5200 by SDS-PAGE, and 5400 by HPLC gel filtration on TSKgel G3000PWXL. Both the amino acid composition and the N-terminal amino acid sequence analysis indicated that acidocin 8912 was a peptide composed of presumably 50 amino acids containing a Lys residue at the N-terminus. The purified acidocin 8912 showed a bactericidal effect on sensitive cells but not a bacteriolytic effect.lld:pubmed
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pubmed-article:1368836pubmed:articleTitlePurification and some properties of acidocin 8912, a novel bacteriocin produced by Lactobacillus acidophilus TK8912.lld:pubmed
pubmed-article:1368836pubmed:affiliationResearch Laboratory, Tamon Sake Brewing Co., Ltd., Hyogo, Japan.lld:pubmed
pubmed-article:1368836pubmed:publicationTypeJournal Articlelld:pubmed
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