Abstract
Broad bean mottle virus can be degraded by dialysis against 1 M -CaCl 2 . The virus RNA is quantitatively precipitated together with some of the protein. Most of the virus protein, free of RNA, can be recovered from the supernatant liquid. The amino acid composition of the protein was determined. End group analyses were performed on the oxidized protein. The C-terminal amino acid was found to be alanine. No N-terminal amino group was found. The tryptic peptides of the oxidized protein were separated by a two-dimensional combination of paper chromatography and electrophoresis. Twenty-eight peptides were detected. From the number of tryptic peptides and the amino acid composition, the molecular weight of the protein subunit was calculated to be 20,500.
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