Carlier Y, Bout D, Capron A, Delvallez M, Martin G, Strecker G, Duriez T
J Gen Microbiol. 1980 Feb;116(2):549-52. doi: 10.1099/00221287-116-2-549.
Listeria specific antigen 2 (Ag2) was purified to within 97% of homogeneity, with a high yield, using both gel filtration and polyacrylamide gel electrophoresis. Ag2 is a glycoprotein. Its isoelectric point is about 4.2. As determined by sodium dodecyl sulphate-polyacrylamid gel electrophoresis, its molecular weight in 16710 +/- 450. Ag2 may aggregate easily since it was previously found in gel filtration in a peak corresponding to a molecular weight of 160000. No enzyme activity has been found in Ag2.
利用凝胶过滤和聚丙烯酰胺凝胶电泳，将李斯特菌特异性抗原2（Ag2）纯化至纯度达97%，且产量高。Ag2是一种糖蛋白，其等电点约为4.2。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定，其分子量为16710±450。由于此前在凝胶过滤中发现Ag2出现在对应分子量为160000的峰中，所以它可能容易聚集。在Ag2中未发现酶活性。
