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dc.contributor.authorHarrington, Dean J.
dc.contributor.authorRussell, R.R.B.
dc.date.accessioned2017-03-10T16:14:44Z
dc.date.available2017-03-10T16:14:44Z
dc.date.issued1994-08
dc.identifier.citationHarrington DJ and Russell RRB (1994) Identification and characterisation of two extracellular proteases of Streptococcus mutans. FEMS Microbiology Letters. 121(2): 237-241.en_US
dc.identifier.urihttp://hdl.handle.net/10454/11595
dc.descriptionNoen_US
dc.description.abstractStreptococcus mutans was shown to produce two extracellular proteases capable of degrading both gelatin and collagen-like substrates. These enzymes have molecular masses of 52 and 50 kDa when analysed by SDS-PAGE. Both enzymes were inhibited by EDTA, but not by a range of other inhibitors with different specificities, indicating that they are metalloproteases. The activity of EDTA-inactivated enzymes could be restored by the addition of manganese and zinc. The identical inhibition and restoration profiles of the two enzymes suggest that one of the proteases may be a degradation product of the other.en_US
dc.language.isoenen_US
dc.subjectStreptococcus mutans; Gelatin; Collagen; Extracellular proteasesen_US
dc.titleIdentification and characterisation of two extracellular proteases of Streptococcus mutansen_US
dc.status.refereedYesen_US
dc.typeArticleen_US
dc.type.versionNo full-text in the repositoryen_US


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