Summary
The coat protein of the RNA containing bacteriophage fr has been hydrolyzed and its amino acid composition determined (Table 1). Furthermore, the protein was split with trypsin and the tryptic peptides were separated by column chromatography on Dowex 1 (Figure 1) and purified by paper chromatography and electrophoresis.
The amino acid composition of all but one tryptic peptide are given in Table 2. The large peptide T13 which is much more difficult to purify than all other peptides, was isolated by several methods. Its amino acid composition is shown in Table 3. All tryptic peptides are compiled in Table 4.
Amino acid sequences have been fully or partially determined for 9 tryptic peptides (Table 5) and the others are presently being investigated.
These findings are compared with the results from other RNA phages, especially f2. It is concluded from the available data that the relationship between the coat proteins of the RNA phages is similar to that between the various naturally occurring strains of tobacco mosaic virus whose amino acid sequences are known.
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Herrn Prof.G. Melchers zum 60. Geburtstag gewidmet.
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Wittmann-Liebold, B. Die Proteinstruktur des RNS-Bakteriophagen fr . Zeitschrift für Vererbungslehre 97, 272–280 (1965). https://doi.org/10.1007/BF02035932
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DOI: https://doi.org/10.1007/BF02035932