A Simple Method for the Biochemical Purification of Ro/SS-A Antigen

Overview

Journal J Immunol Methods

Publisher Elsevier

Specialties Allergy & Immunology
Pathology

Date 1989 Jul 26

PMID 2760465

Citations 4

Authors

D H Wu

A Tavoni

C Garzelli

R Neri

C Vitali

S Bombardieri

Affiliations

Soon will be listed here.

Abstract

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.

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Lu J, Willis A, Sim R Clin Exp Immunol. 1993; 94(3):429-34.

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