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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2001-7-13
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pubmed:abstractText |
Caseinomacropeptide (CMP) is a heterogeneous C-terminal fragment (residues 106 to 169) of bovine milk kappa-casein composed of glycosylated and phosphorylated forms of different genetic variants. We have demonstrated that CMP has growth-inhibitory activity against the oral opportunistic pathogens Streptococcus mutans and Porphyromonas gingivalis and against Escherichia coli. CMP was fractionated using reversed-phase high-performance liquid chromatography (RP-HPLC), and each fraction was tested for activity against S. mutans in a 96-well-plate broth assay. Fractions were characterized by N-terminal sequence analysis and mass spectrometry. The active form of CMP was shown to be the nonglycosylated, phosphorylated kappa-casein (residues 106 to 169) [kappa-casein(106--169)], which we have designated kappacin. Endoproteinase Glu-C was used to hydrolyze CMP, and the generated peptides were separated using RP-HPLC and gel filtration-HPLC and then tested for activity against S. mutans. The peptide Ser(P)(149)kappa-casein-A(138--158) was the only peptide generated by endoproteinase Glu-C digestion that exhibited growth-inhibitory activity. Peptides corresponding to the sequences of the inhibitory peptide Ser(P)(149)kappa-casein-A(138--158) and its nonphosphorylated counterpart kappa-casein-A(138--158) were chemically synthesized and tested for antibacterial activity. The synthetic Ser(P)(149) kappa-casein-A(138--158) displayed growth-inhibitory activity against S. mutans (MIC, 59 microg/ml [26 microM]). The nonphosphorylated peptide, however, did not inhibit growth at the concentrations tested, indicating that phosphorylation is essential for activity.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-10353835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-10399354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-10529530,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-10601790,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-1368296,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-1490908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-1500573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-1607433,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-2015623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-2671666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-3540569,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-7478758,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-7556666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-7643008,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-7647926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-7717888,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-7763995,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-7840870,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-8654396,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-8817876,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-8910482,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-8955673,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-9216247,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-9792701,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11451690-9837932
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0066-4804
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
45
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2309-15
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11451690-Animals,
pubmed-meshheading:11451690-Anti-Bacterial Agents,
pubmed-meshheading:11451690-Caseins,
pubmed-meshheading:11451690-Cattle,
pubmed-meshheading:11451690-Chromatography, High Pressure Liquid,
pubmed-meshheading:11451690-Colony Count, Microbial,
pubmed-meshheading:11451690-Escherichia coli,
pubmed-meshheading:11451690-Mass Spectrometry,
pubmed-meshheading:11451690-Milk,
pubmed-meshheading:11451690-Peptide Fragments,
pubmed-meshheading:11451690-Phosphorylation,
pubmed-meshheading:11451690-Porphyromonas gingivalis,
pubmed-meshheading:11451690-Streptococcus mutans
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pubmed:year |
2001
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pubmed:articleTitle |
Kappacin, a novel antibacterial peptide from bovine milk.
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pubmed:affiliation |
School of Dental Science, The University of Melbourne, Melbourne, Victoria 3000, Australia.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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