In the present study, Ro/SS-A antigen has been isolated from human spleen by a two-step procedure. In the first step most of the non-antigenic material was removed by means of ammonium sulphate precipitation and ion exchange chromatography. The final purification was obtained by passing the Ro/SS-A-containing fractions twice through a Mono Q ion exchange fast protein liquid chromatography (FPLC) column. The purified antigen showed identical immunoreactivity with crude material on CIE and was composed of two polypeptides with a molecular weight of approximately 60,000 and 55,000 respectively on SDS-PAGE, both reacting on Western blotting with a panel of anti-Ro/SS-A antisera. This system permits milligrams of highly purified antigen to be obtained from grams of human spleen.
|Autori:||WU DH; TAVONI A; GARZELLI C; NERI R; VITALI C; BOMBARDIERI S|
|Titolo:||A SIMPLE METHOD FOR THE BIOCHEMICAL PURIFICATION OF RO/SS-A ANTIGEN|
|Anno del prodotto:||1989|
|Digital Object Identifier (DOI):||10.1016/0022-1759(89)90163-4|
|Appare nelle tipologie:||1.1 Articolo in rivista|