RESUMEN
The purification and protein characterization of one of the Cuban isolated strains of hepatitis A virus was carried out. For this, it was necessary to separate the virus from the infected cell by extraction steps with detergents, concentration by ultrafiltration and finally, ultracentrifugation in saccharosoglycerol discontinuous gradient. Protein concentration, as well as the antigenic activity in the different fractions of the gradient were determined. For the protein characterization of the microorganism, those fractions with the greatest specific activity were analyzed by polyacrylamide gel electrophoresis and by Western blotting. It was shown that the viral material was purified and concentrated in the last fractions of the gradient. Bands corresponding to the structural proteins of hepatitis A were observed through electrophoresis and Western blotting.