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dental plaque/protease

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Sivu 1 alkaen 66 tuloksia

Detection of immunoglobulin A1 protease-induced Fab alpha fragments on dental plaque bacteria.

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The mechanisms by which immunoglobulin A1 (IgA1) protease activity may enable bacteria to evade the effect of specific secretory IgA (S-IgA) antibodies are not clear. A possibility which has received indirect experimental support is that bacteria, as a consequence of the protease activity, become

Degradation of the microbial and salivary components participating in human dental plaque formation by proteases elaborated by plaque bacteria.

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Twenty-eight strains of facultative, Gram-positive, sporulating bacilli which produce caseinolytic enzymes were isolated from human early dental plaque. A major component of the extracellular caseinolytic enzymes elaborated by strong producers seemed to be neutral zinc proteases. The extracellular

Relation between the presence of supragingival calculus and protease activity in dental plaque.

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Protease activity was measured in dental plaque collected from patients with or without supragingival calculus. Plaque specimens from the calculus group showed significantly greater protease activity in the presence of 0.05% sodium thioglycollate than did those from the non-calculus group. No

Similar proportions of immunoglobulin A1 (IgA1) protease-producing streptococci in initial dental plaque of selectively IgA-deficient and normal individuals.

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By comparing the initial colonization of cleaned teeth in immunoglobulin A (IgA)-deficient, IgM-compensating individuals with that in normal individuals, no significant difference in the proportion of IgA1 protease-producing streptococci was found. Thus, as one of several bacterial means of immune
Individual colonies of this organism in primary cultures of human dental plaque were distinguished from colonies of other species of black-pigmented Bacteroides by detection of their trypsin-like proteolytic activity using a specific chromogenic enzyme substrate.

Characterization of a trypsin-like protease from the bacterium Bacteroides gingivalis isolated from human dental plaque.

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A trypsin-like, membrane-bound protease from Bacteroides gingivalis was solubilized by Triton X-100 and partially purified by a combination of DEAE-Sepharose and aminophenylmercuric Sepharose chromatography, by taking advantage of the thiol group on the enzyme. The purified enzyme hydrolysed the

Measurement of proteases in human subgingival dental plaque by fluorescence polarization.

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Fluorescence polarization (FP) was examined as a rapid quantitative method to assay the proteases in subgingival plaque. Protease activity was measured by a decrease in FP at 0.5-min intervals over 5 min, using BODIPY-alpha-casein, a protein substrate. To quantitate activity, the least absolute

Of human dental plaque bacteria, Actinomyces viscosus accelerates immunoglobulin A protease secretion in Streptococcus sanguis.

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Adhesin degradation: a possible function for a Prevotella loescheii protease?

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Prevotella loescheii PK1295 produces at least 3 proteases that are separable by isoelectric focusing. One of these proteases, an enzyme with an isoelectric point at 8.5 and an M(r) of 36,000, hydrolyzes the fimbria-associated adhesin on P. loescheii responsible for coaggregation with Streptococcus

Evaluation of human oral organisms and pathogenic Streptococcus for production of IgA protease.

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IgA protease is a proteolytic enzyme found in whole human saliva and in dental plaque that cleaves both secretory and myeloma IgA of human origin to yield intact Fabalpha and Fcalpha fragments. To determine which bacteria are capable of producing this enzyme, we have examined a variety of strains

The effect of fluoride on Streptococcus sanguis 7863 IgA1 protease production and activity.

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Fluoride was found to affect the production of the bacterial IgA1 protease but to have no effect on IgA1 protease activity. The concentrations of fluoride that do affect Streptococcus sanguis growth and IgA1 protease production are higher than those normally seen in vivo under normal circumstances.

Proteolytic degradation of oral biofilms in vitro and in vivo: potential of proteases originating from Euphausia superba for plaque control.

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This paper deals with enzymatic removal of dental plaque, in vitro as well as in vivo, using proteases from the Antarctic krill shrimp (Euphausia superba), referred to as Krillase. Krillase exhibits both endo- and exopeptidase activity but has no microbicidal effect. In model systems with pure
Plaque formation and gingival inflammation were found in ODU plaque-susceptible rats. A study was performed to determine the relationship between the presence of bradykinin in gingival tissue and the inflammatory capacity of rat plaque. Bradykinin content in gingival tissue and the bradykinin
Haem (iron protoporphyrin IX) is both an essential growth factor and a virulence regulator of the periodontal pathogens Porphyromonas gingivalis and Prevotella intermedia, which acquire it through the proteolytic degradation of haemoglobin and other haem-carrying plasma proteins. The haem-binding

Slot immunoblot assay for detection and quantitation of periodontal disease-associated microorganisms in dental plaque.

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A rapid method for qualitative and quantitative detection of specific oral microorganisms from subgingival dental plaque is described. Plaque samples were suspended in phosphate-buffered saline containing protease inhibitors and 0.5% formaldehyde, briefly sonicated to disperse bacterial aggregates,
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