Identification of a 1,3-α glucosyltransferase involved in insoluble glucan synthesis by a serotype c strain of Streptococcus mutans

Kenney, A

doi:10.1016/0378-1097(83)90004-6

Cited by 10 publications

(13 citation statements)

References 11 publications

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“…The 99 kDa GTase may be a breakdown product of the 156 kDa cell-associated GTase. In this regard, Kenney & Cole (1983) isolated an extracellular 153 kDa GTase that produced insoluble glucan from sucrose as well as a water-soluble-glucan synthesizing 162 kDa dextransucrase from S. mutans strain 3209 (serotype c). The 153 kDa GTase that synthesizes water-insoluble glucan appears to be similar to our cell-associated GTase in terms of molecular mass and in the nature of the glucan produced from sucrose.…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of Cell-associated Glucosyltransferase Synthesizing Water-insoluble Glucan from Serotype c Streptococcus mutans

et al. 1989

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Strains of Streptococcus mutans (serotypes c, e and f) were found to possess high levels of glucosyltransferase (GTase) activity, both cell-associated and in the culture medium, when grown in either sucrose-free or sucrose-containing broth media. The cell-associated GTase of S. mutans MT8148 (serotype c) was effectively extracted by treatment with 8 M-urea at 25 "C for 1 h. Approximately 95% of the GTase activity was solubilized by this treatment. The crude extract was purified by DEAE-Sephacel and hydroxylapatite column chromatography. For comparison, extracellular GTase was also purified from the culture supernatant of the same strain by ammonium sulphate precipitation, chromatofocusing and hydroxylapatite chromatography. The molecular masses of the cell-associated and extracellular GTase proteins were similar (156 kDa) as determined by SDS-PAGE. However, the pH optima for maximum GTase activity were different: pH 6.7 to 7.0 for the cell-associated enzyme and pH 5.5 to 6.5 for the extracellular enzyme. The product of cell-associated GTase from sucrose was almost exclusively water-insoluble glucan. On the other hand, extracellular GTase produced mainly water-soluble glucan from sucrose. This indicates that GTase synthesizing water-insoluble glucan is present primarily in a cell-associated form in serotype c S. mutans. Insoluble glucan synthesis by the cellassociated GTase from sucrose was not enhanced by addition of primer dextran T10 to the reaction mixture. The extracellular and cell-associated GTases were immunologically unrelated as determined by ELISA using monoclonal antibodies.

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Section: Discussionmentioning

confidence: 99%

Purification and Characterization of Cell-associated Glucosyltransferase Synthesizing Water-insoluble Glucan from Serotype c Streptococcus mutans

et al. 1989

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“…rattus (b) and S . mutans (c, e,f), two glucosyltransferases (GTF-I and GTF-S) and fructosyltransferases are supposed to be involved in the synthesis of adherent and insoluble polymer (Carlsson, 1970;Scales et al, 1975 ;Kenny & Cole, 1983). S. mutans serotype c strains have been most frequently isolated from human dental plaque (Hamada et al, 1976;Loesche & Grenier, 1976) and the extracellular GTF-S, which synthesizes soluble 1,6-a-~-glucan with some 1,3-a-linked glucosyl residues, has been purified and characterized (Kuramitsu, 1975 ;Mohan et al, 1979;Mukasa et al, 1982b;Baba et al, 1986).…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of Cell-associated Glucosyltransferase Synthesizing Insoluble Glucan from Streptococcus mutans Serotype c

Mukasa

Shimamura²,

Tsumori³

1989

Microbiology

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“…The fraction of dextransucrase in the 159 kOa form increased with the age of the preparation at the expense of the 176 kOa form, a pattern also found for different molecular-weight forms of S. sanguis dextran sucrase [123] and S. nutans glucansucrases [180,294]. The crude enzyme used for Table I was mostly in the 159 kDa form, while the purified en- Table I where K2 = was the same for both preparations.…”

Section: Methodssupporting

confidence: 51%

“…He also found [294] more of a 74 kDa glucan-binding protein that had no glucansucrase activity was formed in the absence of phenylmethylsulfonyl fluoride than in its presence. Kenny and Cole [180] found that a 138 kDa glucansucrase was derived from proteolysis of a 162 kDa form.…”

Section: Proteolysismentioning

confidence: 99%

Purification, surfactant stabilization, molecular weight studies, and divalent metal ion kinetics of dextransucrase from Leuconostoc mesenteroides NRRL B-512F

Miller¹

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Identification of a 1,3-α glucosyltransferase involved in insoluble glucan synthesis by a serotype c strain of Streptococcus mutans

Cited by 10 publications

References 11 publications

Purification and Characterization of Cell-associated Glucosyltransferase Synthesizing Water-insoluble Glucan from Serotype c Streptococcus mutans

Purification and Characterization of Cell-associated Glucosyltransferase Synthesizing Water-insoluble Glucan from Serotype c Streptococcus mutans

Purification and Characterization of Cell-associated Glucosyltransferase Synthesizing Insoluble Glucan from Streptococcus mutans Serotype c

Purification, surfactant stabilization, molecular weight studies, and divalent metal ion kinetics of dextransucrase from Leuconostoc mesenteroides NRRL B-512F

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