The alpha-hemolysin of Streptococcus gordonii is hydrogen peroxide
The alpha-hemolysin of Streptococcus gordonii is hydrogen peroxide
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DOI：
10.1128/iai.64.9.3853-3857.1996
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发表时间：
1996-09-01
影响因子：
3.1
通讯作者：
Stinson, MW
中科院分区：
文献类型：
--
作者：
Barnard, JP;Stinson, MW
草绿色群链球菌的α-溶血素可导致完整红细胞变绿，是潜在的毒力因子，也是实验室鉴定这些细菌的重要标准；然而，它从未被纯化和表征。戈登链球菌 CH1 的 α-溶血素引起绵羊血红蛋白 A(403)、A(430)、A(578) 和 A(630) 的特征性变化。开发了一种分光光度测定法，用于监测有机溶剂萃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。 α-溶血素在以下方面与过氧化氢相同：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、过氧化氢酶失活、溶解度不同、无法吸附离子交换色谱树脂以及在反相 HPLC 柱上的保留时间。 HPLC 分级的废培养基中存在的过氧化氢的量足以解释观察到的所有α溶血活性。
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 A(403), A(430), A(578), and A(630) 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 nas 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.