Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1985-10-22
pubmed:abstractText
Fluoride was found to be a potent inhibitor of bovine lactoperoxidase and of salivary peroxidase at acid pH values. Inhibition was reversible at neutral pH, and appeared to involve HF binding by the enzyme. Fluoride inhibition of lactoperoxidase occurred with all reductants tested, including thiocyanate, iodide, and guaiacol. Fluoride concentrations for 50% inhibition of enzymatic activity with iodide as reductant were: less than 0.05 mM at a pH value of 4.0, 0.3 mM at 5.0, 4.0 mM at pH 6.0, and more than 10.0 mM at pH 7.0. Salivary peroxidases were found to have lower pH optima but to be approximately as sensitive to acid-dependent fluoride inhibition as was purified bovine lactoperoxidase. The findings suggest that the fluoride in dental plaque may be inhibitory to the antimicrobial peroxidase system.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
D
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-0345
pubmed:author
pubmed:issnType
Print
pubmed:volume
64
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1211-3
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
pH-dependent fluoride inhibition of peroxidase activity.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.