Purification of NADH: hypothiocyanite oxidoreductase in Streptococcus sanguis.
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 ultrafiltration and anion-exchange chromatography) revealed one fraction of 125 +/- 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.
Courtois
P H
PH
Laboratory of Stomatology, Faculty of Medicine, Free University of Brussels, Belgium.
Pourtois
M
M
D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D009055:Mouth / Q000382:microbiology; D009243:NAD / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D009249:NADP / Q000378:metabolism; D013298:Streptococcus sanguis / Q000201:enzymology* / Q000302:isolation & purification; D013861:Thiocyanates / Q000378:metabolism
D046911:Macromolecular Substances; D013861:Thiocyanates; D009243:NAD; D009249:NADP; C014607:hypothiocyanite ion; D009247:NADH, NADPH Oxidoreductases; C103602:NADH-hypothiocyanite oxidoreductase