HONG-KONG INFLUENZA HEMAGGLUTININ LIGHT CHAIN - AMINO-ACID SEQUENCE OF CYANOGEN-BROMIDE FRAGMENT-CN3 AND FRAGMENT-CN4 AND THE N-TERMINAL 45 RESIDUES

The light chain (HA2) from the hemagglutinin of the Hong Kong influenza variant A/Memphis/102/72 was cleaved with CNBr to yield 4 peptides, CN1, CN2, CN3 and CN4. The amino acid compositions of all 4 peptides, the amino acid sequences of the 2 smallest peptides, CN3 and CN4, and the sequence of the N[amine]-terminal 20 residues of CN1 were determined. Automated sequence analysis of the N-terminal 45 residues of whole HA2 shows that CN4 accounts for the first 17 residues. These findings show that the previously reported highly conserved 12-residue N-terminal sequence of influenza virus hemagglutinin light chains can be extended to include at least the N-terminal 24 residues. The significance of 5 aromatic residues in this highly conserved N-terminal area is discussed in relation to the published circular dichroic spectra of different hemagglutinins.