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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1995-11-21
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pubmed:abstractText |
Delmopinol is a new surface-active agent which can reduce plaque formation and gingivitis. This study was aimed to analyze whether delmopinol (0.0032-0.65 mM) interferes with the activity of two surface-active oral antimicrobial enzymes, salivary peroxidase and lysozyme. In addition to human whole saliva (pH 5.0 and 6.0), the experiments were done in 0.1 M phosphate buffer (pH 6.0) with purified lactoperoxidase (LPO) and myeloperoxidase (MPO). LPO and MPO were significantly inhibited in buffer by delmopinol concentrations > 6.5 mM and > or = 3.2 mM, respectively. No such inhibition was found for total peroxidase activity in mixed saliva. In vitro, delmopinol was found to desorb surface-bound peroxidases in an active form to the liquid phase. In further analyses, the possible effect of delmopinol on peroxidase-generated hypothiocyanite (HOSCN/OSCN-) was studied in saliva and buffer. No effect was found in buffer, but salivary HOSCN/OSCN- declined significantly with 6.5 mM delmopinol. This was obviously due to an enhanced decay of hypothiocyanite, rather than its reduced rate of formation. No delmopinol-related inhibition of lysozyme occurred in saliva or buffer. The results suggest that high concentration (6.4 mM -0.2%) of delmopinol may lower the concentrations of antimicrobial HOSCN/OSCN- in saliva but has no effect on human lysozyme.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
D
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Infective Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Buffers,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Lactoperoxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Morpholines,
http://linkedlifedata.com/resource/pubmed/chemical/Muramidase,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidases,
http://linkedlifedata.com/resource/pubmed/chemical/Salivary Proteins and Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Surface-Active Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Thiocyanates,
http://linkedlifedata.com/resource/pubmed/chemical/delmopinol,
http://linkedlifedata.com/resource/pubmed/chemical/hypothiocyanite ion
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0909-8836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
103
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
247-52
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7552957-Anti-Infective Agents,
pubmed-meshheading:7552957-Buffers,
pubmed-meshheading:7552957-Enzyme Inhibitors,
pubmed-meshheading:7552957-Humans,
pubmed-meshheading:7552957-Lactoperoxidase,
pubmed-meshheading:7552957-Morpholines,
pubmed-meshheading:7552957-Muramidase,
pubmed-meshheading:7552957-Peroxidase,
pubmed-meshheading:7552957-Peroxidases,
pubmed-meshheading:7552957-Saliva,
pubmed-meshheading:7552957-Salivary Proteins and Peptides,
pubmed-meshheading:7552957-Surface-Active Agents,
pubmed-meshheading:7552957-Thiocyanates
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pubmed:year |
1995
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pubmed:articleTitle |
Effects of delmopinol on antimicrobial peroxidase systems and lysozyme in vitro and in human whole saliva.
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pubmed:affiliation |
Department of Cariology, University of Turku, Finland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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