@article{mbs:/content/journal/jgv/10.1099/0022-1317-35-3-425, author = "Chlumecka, Vera and D’Obrenan, P. and Colter, J. S.", title = "Isoelectric Focusing Studies of Mengo Virus Variants, their Protein Structure Units and Constituent Polypeptides", journal= "Journal of General Virology", year = "1977", volume = "35", number = "3", pages = "425-437", doi = "https://doi.org/10.1099/0022-1317-35-3-425", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-35-3-425", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "SUMMARY Virions of three plaque variants (L-, M- and S-) of Mengo virus, which assume a bimodal distribution when subjected to isoelectric focusing in sucrose-stabilized pH gradients containing 0.5% Brij 35, were found to band in a single peak (at pH 8.1 to 8.4) when focused under the same conditions in gradients supplemented with 6 m-ethylene glycol. An examination of m-Mengo virions, isoelectric at pHs 4.7 and 8.4 in sucrose-stabilized gradients, showed that the two populations were indistinguishable on the basis of specific infectivity, polypeptide composition and sedimentation characteristics, but differed in their ability to agglutinate human erythrocytes. When pH-inactivated virions were subjected to isoelectric focusing, three well defined peaks were produced, one of which was found to correspond to the well characterized 13.4S subunit of Mengo virus, and the other two — on the basis of compositional analysis — to virions that had lost some of their 13.4S structure units. No difference in electrophoretic behaviour was found among the 13.4S subunits isolated from the three Mengo variants — all three were found to be isoelectric at pH 5.85 to 6.00. Analysis, by isoelectric focusing, of the four structural polypeptides (α, β, γ, δ) isolated from L-, M- and S-Mengo failed to reveal any significant differences among the three variants.", }