戈登链球菌的α-溶血素是过氧化氢。
The alpha-hemolysin of Streptococcus gordonii is hydrogen peroxide.
作者信息
Barnard J P, Stinson M W
机构信息
Department of Microbiology, School of Medicine and Biomedical Sciences, State University of New York at Buffalo 14214-3000, USA.
出版信息
Infect Immun. 1996 Sep;64(9):3853-7. doi: 10.1128/iai.64.9.3853-3857.1996.
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.
草绿色链球菌的α-溶血素可使完整红细胞发生溶血，是一种潜在的毒力因子，也是实验室鉴定这些细菌的重要标准；然而，它从未被纯化和鉴定过。戈登链球菌CH1的α-溶血素可使绵羊血红蛋白的A403、A430、A578和A630发生特征性变化。开发了一种分光光度法，用于监测在有机溶剂提取和反相高效液相色谱（HPLC）分离过程中α-溶血素的纯化情况。就其对红细胞血红蛋白的影响、链球菌的氧依赖性合成、对蛋白酶不敏感、被过氧化氢酶灭活、溶解性差异、不吸附于离子交换色谱树脂以及在反相HPLC柱上的保留时间而言，α-溶血素与过氧化氢相同。HPLC分级分离的用过的培养基中存在的过氧化氢量足以解释观察到的所有α-溶血活性。
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