Purification of NADH: Hypothiocyanite oxidoreductase in Streptococcus sanguis

Courtois, Philippe; Pourtois, Michel

doi:doi/10.1006/bmme.1996.0019

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Purification of NADH: Hypothiocyanite oxidoreductase in Streptococcus sanguis

par Courtois, Philippe

;Pourtois, Michel

Référence Biochemical and molecular medicine, 57, 2, page (134-138)
Publication Publié, 1996

Article révisé par les pairs

Résumé :

NADH: hypothiocyanite oxidoreductase (NHOR) activity, found in some oral Streptococci, is postulated to protect these microorganisms against salivary peroxidase-produced hypothiocyanite. NHOR, however, has not been purified so far. The purification of NHOR from crude extracts of Streptococcus sanguis NCTC 7863 strain (by ultrafiltation and anion-exchange chromatography) revealed one fraction of 125 ± 1 kDa. However, SDS-PAGE electrophoresis provided a single protein of 21.1 ± 1.2 kDa. This last discovery suggests that NHOR enzyme is a hexameric complex having six subunits.

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