Purification of measles virus H polypeptide and of F polypeptide.

Measles virus was disrupted by Tween 80 and ether and subjected to isoelectric focusing in granular gel. The two surface envelope polypeptides, the one showing haemagglutinating activity (H) and the one making up the structural basis of the haemolytic and fusion activity (F) banded together at pH 5.2. The two envelope polypeptides were also isolated together after adsorption to a Lentil-lectin column. Separation of the two polypeptides was performed by gel filtration on Sephadex G-150 in the presence of 8 M urea. After separation both the H and F polypeptides fixed to the lectin column. It was demonstrated that the column, after having fixed the two polypeptides, absorbed anti-H and anti-F antibodies from a rabbit anti-measles virus immune serum. Thus the antigenic reactivity of the isolated surface polypeptides remained intact.