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从BALB/c小鼠口腔分离出的细菌对唾液蛋白的蛋白水解活性。

Proteolytic activity of bacteria isolated from the oral cavities of BALB/c mice toward salivary proteins.

作者信息

Dumas C, Champagne A, Lavoie M C

出版信息

J Dent Res. 1987 Jan;66(1):62-4. doi: 10.1177/00220345870660011301.

Abstract

The proteolytic activities of 350 bacterial isolates from different sites (saliva, tongue, teeth, and mucosa) of the oral cavities of BALB/c mice were tested against different proteins found in saliva (immunoglobulins A, M, G, albumin, lysozyme, mucin, lactoferrin, and lactoperoxidase), some of which are considered to possess antibacterial activity. The results indicate that: (1) lysozyme, lactoferrin, and lactoperoxidase are hydrolyzed by from 46 to 70% of the indigenous flora of the oral cavities of BALB/c mice; (2) IgA and IgM appeared less sensitive to the proteolytic activities of these strains than did the other proteins tested; (3) the colonization of the oral cavity does not seem to be correlated with the proteolytic activity; and (4) the presence of specific Ig proteases is relatively scarce within this population.

摘要

对来自BALB/c小鼠口腔不同部位(唾液、舌头、牙齿和黏膜)的350株细菌分离株针对唾液中发现的不同蛋白质(免疫球蛋白A、M、G、白蛋白、溶菌酶、粘蛋白、乳铁蛋白和乳过氧化物酶)的蛋白水解活性进行了测试,其中一些蛋白质被认为具有抗菌活性。结果表明:(1)溶菌酶、乳铁蛋白和乳过氧化物酶被BALB/c小鼠口腔固有菌群的46%至70%水解;(2)与其他测试蛋白质相比,IgA和IgM对这些菌株的蛋白水解活性似乎不太敏感;(3)口腔定植似乎与蛋白水解活性无关;(4)在这一群体中,特异性Ig蛋白酶相对较少。

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