The effects of various reagents on the disassembly of potato virus Y are described and discussed. The virus can be disassembled in acetic acid, guanidine, LiCl, NaSCN and in a variety of other salts but is stable in NaCl, CsCl and NaF. Polymerization of coat protein from pH 3 to 11 in 0.1 to 0.5 -NaCl was followed by analytical centrifugation. Extensive polymerization (with major proportions being 100 to 200S) was only found between pH 6 and pH 9 in 0.1 -NaCl. A nucleoprotein with structural, density and stability properties similar to those of the virus, but less than one third as long, was obtained by the addition of RNA to polymerized protein at 20 °C at pH 7 to 8 at very low ionic strength. Possible modes of assembly are presented.


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