Summary
Foot-and-mouth disease virus (FMDV) degraded at low ionic-strength as well as purified viral protein (E 1%276 mμ =11.1; max.276 mμ/min.250 mμ =3.0) were examined for heterogeneity by polyacrylamide gel electrophoresis. These preparations, each 8M in urea, 1% in sodium dodecylsulfate and 0.14M in mercaptoethanol (ME), all gave rise to a single, fast-moving protein zone when electrophoresed in 6% acrylamide gels not containing urea. In smaller pore-size gels (7.5 and 10%), slower-migrating zones were also present. When urea was present in the 6% gels, slower zones were always present when the protein was reduced with 0.14M ME. However, only the fast zone was seen after treatment with 4M ME. These findings indicate that the slower-migrating zones are due to discrete classes of aggregated protein and that FMDV structural protein is comprised of an electrophoretically homogeneous polypeptide.
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Vande Woude, G.F., Bachrach, H.L. Evidence for a single structural polypeptide in foot-and-mouth disease virus. Archiv f Virusforschung 23, 353–361 (1968). https://doi.org/10.1007/BF01242131
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DOI: https://doi.org/10.1007/BF01242131