Purification of Haemagglutinin and Neuraminidase from Influenza Virus Strain 3QB and Isolation of a Peptide from an Antigenic Region of Haemagglutinin

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Abstract
Methods were developed for the purification of the surface, membrane-bound glycoproteins hemagglutinin and neuraminidase of influenza virus strain 3QB, in antigenically active forms. The methods employed in the purification included selective removal of the neuraminidase with the proteinase, Bromelain and subsequent disruption of the residual virus particle with the detergent Sarkosyl to release the hemagglutinin. Using techniques for proteolytic digestion of intact, native proteins an antigenically active peptide was isolated from the purified hemagglutinin, the surface glycoprotein against which the major antigenic response is directed. The amino acid composition of the peptide was determined. This was a 16-residue peptide with amino-terminal isoleucine and composition Ile1 Val1 Asx2 Thr1 Ser2 Glx2 Pro1 Gly3 Ala1 Leu1 Lys1.