par Carlier, Yves 
;Bout, D;Capron, André;Delvallez, M;Martin, Genevieve San;Strecker, G;Duriez, T
Référence Journal of general microbiology, 116, 2, page (549-552)
Publication Publié, 1980-02
;Bout, D;Capron, André;Delvallez, M;Martin, Genevieve San;Strecker, G;Duriez, TRéférence Journal of general microbiology, 116, 2, page (549-552)
Publication Publié, 1980-02
Article révisé par les pairs
| Résumé : | 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. |
