Purification and biochemical properties of a bacteriocin from Actinobacillus actinomycetemcomitans

Purification and biochemical properties of a bacteriocin from Actinobacillus actinomycetemcomitans
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伴放线放线杆菌细菌素的纯化和生化特性

DOI:
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发表时间:
1987
影响因子:
3.1
通讯作者:
B. F. Hammond
B. F. Hammond
中科院分区:
医学2区
文献类型:
--
作者:
R. Stevens;S. Lillard;B. F. Hammond

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某些伴放线放线杆菌的提取物对血链球菌等有抑制作用。血吸虫ATCC 10556。从A.用制备型等电聚焦、Sephadex G-100凝胶过滤层析和制备型聚丙烯酰胺凝胶电泳(PAGE)等方法对具有抑菌活性的伴放线菌声波提取物进行了纯化。所得分离的蛋白质集中在pH 6.1至6.3下,在阴离子非解离PAGE分析中显示为单一条带。该蛋白质可分离为分子量为50,000和70,000的两个亚基,经PAGE分析可分辨。与粗声波提取物起始材料相比,在纯化的抑制蛋白中观察到比活性增加了1,758倍。本文还对A.伴放线菌提取物是细菌素的特征。因此,我们建议将抑制蛋白命名为放线杆菌素。
Extracts of certain strains of Actinobacillus actinomycetemcomitans are inhibitory to strains of Streptococcus sanguis such as S. sanguis ATCC 10556. The isolation of a protein from an A. actinomycetemcomitans sonic extract which copurified with the inhibitory activity was accomplished by preparative isoelectric focusing, Sephadex G-100 gel filtration chromatography, and preparative polyacrylamide gel electrophoresis (PAGE). The resulting isolated protein, which focused at a pH of 6.1 to 6.3, appeared as a single band in anionic nondissociating PAGE analysis. This protein could be dissociated into two subunits with molecular weights of 50,000 and 70,000, which were resolvable by PAGE analysis. A 1,758-fold increase in specific activity was seen in the purified inhibitory protein compared with the crude sonic extract starting material. The properties of the inhibitory activity in the A. actinomycetemcomitans extract are characteristic of a bacteriocin. Accordingly, we propose the name actinobacillicin for the inhibitory protein.
伴放线放线杆菌的选择性培养基以及该微生物在幼年牙周炎中的发病率。
DOI: 10.1902/jop.1981.52.10.593
发表时间: 1981
影响因子: 4.3
作者:
Mandell,RL;Socransky,SS
通讯作者: Socransky,SS