The alpha-hemolysin of Streptococcus gordonii is hydrogen peroxide.
The alpha-hemolysin of viridans group streptococci, which causes greening of intact erythrocytes, is a potential virulence factor as well as an important criterion for the laboratory identification of these bacteria; however, it has never been purified and characterized. The alpha-hemolysin of Streptococcus gordonii CH1 caused characteristic shifts in the A403, A430, A578, and A630 of sheep hemoglobin. A spectrophotometric assay was developed and used to monitor purification of alpha-hemolysin during extraction in organic solvents and separation by reverse-phase high-performance liquid chromatography (HPLC). The alpha-hemolysin was identical to hydrogen peroxide with respect to its effects on erythrocyte hemoglobin, oxygen-dependent synthesis by streptococci, insensitivity to proteases, inactivation by catalase, differential solubility, failure to adsorb to ion-exchange chromatography resins, and retention time on a reverse-phase HPLC column. The amount of hydrogen peroxide present in HPLC-fractionated spent culture medium was sufficient to account for all alpha-hemolytic activity observed.
Barnard
J P
JP
Department of Microbiology, School of Medicine and Biomedical Sciences, State University of New York at Buffalo 14214-3000, USA.
Stinson
M W
MW
D000818:Animals; D004912:Erythrocytes / Q000187:drug effects*; D006460:Hemolysin Proteins / Q000737:chemistry*; D006461:Hemolysis; D006861:Hydrogen Peroxide / Q000633:toxicity*; D066298:In Vitro Techniques; D012756:Sheep; D013291:Streptococcus / Q000472:pathogenicity*
D006460:Hemolysin Proteins; D006861:Hydrogen Peroxide