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A Protein Subunit Of Bromegrass Mosaic Virus


, : A Protein Subunit Of Bromegrass Mosaic Virus. Journal of Molecular Biology 8: 314-323

The protein and RNA of bromegrass mosaic virus were separated from each other by dialysis of the virus against 1 [image]-calcium chloride. In this medium the virus is degraded, the RNA is quantitatively precipitated and there remains a supernatant solution of viral protein. The protein obtained in this way was soluble in various buffers in the pH range 5.5 to 6.5 and exhibited a single symmetrical sedimenting boundary in the ultracentrifuge. Its molecular weight was 40,000 [plus or minus] 2,000 as determined by the Ehrenberg method of approach to sedimentation equilibrium. Amino acid analyses indicated that there were about 52 lysyl plus arginyl residues per molecular weight of 40,000. Tryptic hydrolysis of urea-denatured protein yielded 23 soluble peptides and an insoluble residue amounting to about 20% by weight of the intact protein. From the number of soluble tryptic peptides and an assumed number of tryptic peptides in the insoluble residue it was concluded that the molecular weight of the protein subunit of bromegrass mosaic virus was slightly greater than 20,000 and that the protein moiety obtained by treatment with 1 [image]-CaCl2 was a relatively stable dimer of the subunit. Partial separation of the soluble peptides resulting from tryptic hydrolysis was achieved on a preparative scale by column chromatography.

US$19.90

PMID: 14126299

DOI: 10.1016/S0022-2836(64)80140-6


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