THE enzymic activity of influenza viruses, recently characterized in chemical terms for the substrate ovomucin1, was first suggested by Hirst2, who showed that, following the agglutination of erythrocytes, the virus was eluted spontaneously, leaving the cells inagglutinable by the same strain. Burnet, McCrea and Stone3 found that cells from which one strain had become eluted were still agglutinable by certain other strains. The arrangement of influenza A and B, mumps and Newcastle disease viruses in the order of their progressive action on cellular receptors was termed the ‘receptor gradient’. Elucidation of this unique enzyme-substrate relationship, characterized by the varying extent of interaction, is limited by the qualitative nature of the biological method. The finding of Hanig4 that, following treatment with the PR8 strain of influenza virus, the electrophoretic mobility of human erythrocytes was markedly reduced, suggested a biophysical approach to the problem.