CHARACTERIZATION OF STAPHYLOCOCCAL GAMMA-LYSIN
CHARACTERIZATION OF STAPHYLOCOCCAL GAMMA-LYSIN
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DOI：
10.1099/00221287-138-5-923
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发表时间：
1992-05-01
期刊：
影响因子：
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通讯作者：
ARBUTHNOTT, JP
中科院分区：
文献类型：
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作者：
CLYNE, M;BIRKBECK, TH;ARBUTHNOTT, JP
通过肝素-琼脂糖和羟基磷灰石层析的组合从金黄色葡萄球菌菌株Smith 5 R和PG 23（中毒性休克综合征分离株）纯化γ-赖氨酸。两种菌株均产生两种溶血组分，命名为gamma-1和gamma-2。虽然每种成分都具有弱溶血性，但它们在家兔、绵羊和人血液中协同作用，增强溶血作用。兔和绵羊红细胞比人红细胞对γ-溶素裂解更敏感。γ-1的分子量为32 kDa，其pl值为9.4。γ-2的分子量为36 kDa，pI值为9.3。虽然胰蛋白酶和木瓜蛋白酶与γ-2协同作用以诱导溶血增加，但与γ-1没有观察到这种协同作用。此外，蛋白酶抑制剂起到抑制γ-1和γ-2之间的协同作用的作用。这些发现表明γ-1可能是一种蛋白酶。
Gamma-Lysin was purifed from Staphylococcus aureus strains Smith 5R and PG23 (a toxic shock syndrome isolate) by a combination of heparin-agarose and hydroxylapatite chromatography. Both strains produced two haemolytic components, designated gamma-1 and gamma-2. Though each component was weakly haemolytic they acted synergistically to potentiate haemolysis on rabbit, sheep and human blood. Rabbit and sheep erythrocytes were more sensitive to lysis by gamma-lysin than human erythrocytes. The molecular mass of gamma-1 was 32 kDa and its pl value was 9.4. Gamma-2 had a molecular mass of 36 kDa and a pI value of 9.3. While both trypsin and papain acted synergistically with gamma-2 to induce increased haemolysis, no such synergism was seen with gamma-1. Also, protease inhibitors acted to inhibit synergism between gamma-1 and gamma-2. These findings suggest that gamma-1 could be a protease.