Lactoferrin interaction with Actinobacillus actinomycetemcomitans.
Lactoferrin interaction with Actinobacillus actinomycetemcomitans.
复制标题
乳铁蛋白与放线放线杆菌的相互作用。
DOI：
--
复制
发表时间：
1995
影响因子：
--
通讯作者：
A. Naidu
中科院分区：
文献类型：
--
作者：
K. R. Afugupalli;Sotirios Kalfas;Stig Edwardsson;A. Naidu
用~(125)I标记的蛋白质结合实验研究了乳铁蛋白与伴生放线杆菌的相互作用。人和牛乳铁蛋白的结合在1h内达到最大值，乳铁蛋白与细菌的结合是pH依赖性和可逆性的。Scatchard分析表明，细菌上存在两种不同类型的结合位点，一种具有高亲和力常数kα约8.8×10(-7)M，另一种具有低亲和力常数kα约1.8×10(-6)M。处于指数生长期的细菌显示出比处于稳定期的细胞更高的结合力。在含有血清和/或裂解红细胞的培养液中生长的细菌与乳铁蛋白的结合程度较小。在竞争结合试验中，热灭活的血清、裂解的红细胞和其他蛋白质，如粘蛋白和层粘连蛋白，抑制乳铁蛋白与伴生放线菌的结合。放线菌伴生菌的细胞膜和外膜的十二烷基硫酸钠聚丙烯酰胺凝胶电泳和Western印迹分析显示，乳铁蛋白反应蛋白在29 kDa和16.5 kDa处有条带。29 kDa条带为可热修饰的乳铁蛋白反应型，其相对分子质量为34 kDa。该菌经蛋白酶K处理的细胞膜和脂多糖均不与乳铁蛋白发生反应。这些数据表明乳铁蛋白与伴生放线菌的外膜蛋白具有特异性的相互作用。
The interaction of lactoferrin with Actinobacillus actinomycetemcomitans was examined in a 125I-labeled protein binding assay. The binding of human and bovine lactoferrins reached maximum within 1 h. Lactoferrin binding to the bacterium was pH-dependent and reversible. Scatchard analysis indicated the existence of two different types of binding sites on the bacterium, one with a high affinity constant k alpha approximately 8.8 x 10(-7) M) and the other with a low one (k alpha approximately 1.8 x 10(-6) M). Bacteria in the exponential phase of growth showed higher binding than cells in the stationary phase. Bacteria grown in medium containing serum and/or lysed erythrocytes bound lactoferrin to a lesser extent. Heat-inactivated serum, lysed erythrocytes and other proteins such as mucin and laminin inhibited lactoferrin binding to A. actinomycetemcomitans in a competitive binding assay. Sodium dodecyl sulfate polyacrylamide-gel electrophoresis and Western blot analysis of the cell envelope as well as the outer membrane of A. actinomycetemcomitans revealed lactoferrin-reactive protein bands at 29 kDa and 16.5 kDa. The 29-kDa band displayed a heat-modifiable lactoferrin-reactive form with a molecular weight of 34 kDa. Neither proteinase K-treated cell envelope nor lipopolysaccharide of this bacterium showed reactivity with lactoferrin. These data suggests a specific interaction of lactoferrin with outer membrane proteins of A. actinomycetemcomitans.
影响因子：
4.3
作者：
FRIEDMAN, SA;MANDEL, ID;HERRERA, MS
通讯作者：
HERRERA, MS