Abstract
Knight and Lauffer1 reported that nucleic acid-free protein, obtained by degrading tobacco mosaic virus in alkaline solutions, tended to aggregate to form rapidly sedimenting particles. Schramm2 showed that nucleic acid-free rod-like particles resembling tobacco mosaic virus but void of activity could be obtained by allowing the protein, isolated after mild alkaline treatment of the virus, to aggregate. The structure of these nucleic acid-free protein rods has been shown by Franklin3 to be similar to that of the intact virus, except for the absence of nucleic acid. In other words, the protein sub-units are arranged in a giant helix around a hollow core.
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References
Knight, C. A., and Lauffer, M. A., J. Biol. Chem., 144, 411 (1942).
Schramm, G., Naturwiss., 31, 94 (1943).
Franklin, R. E., Biochim. Biophys. Acta, 18, 313 (1955).
Harrington, W. U. F., and Schachman, H. K., Arch. Biochem. Biophys., 65, 278 (1956).
Doty, Paul, and Myers, G. E., Disc. Farad. Soc., 13, 51 (1953).
Murayama, M., Fed. Proc., 15, 318 (1956).
Fessler, J. H., Fed. Proc., 16, 37 (1957).
Goddard, E. D., Hoeve, C. A. J., and Benson, G. C., J. Phys. Chem., 61, 593 (1957).
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LAUFFER, M., ANSEVIN, A., CARTWRIGHT, T. et al. Pollymerization–Depolymerizatic Tobacco Mosaic Virus Protein. Nature 181, 1338–1339 (1958). https://doi.org/10.1038/1811338b0
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DOI: https://doi.org/10.1038/1811338b0
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