Purification in a functional form of the terminal protein of Bacillus subtilis phage phi 29.
- 1 March 1984
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 81 (6), 1639-1643
- https://doi.org/10.1073/pnas.81.6.1639
Abstract
Phage .vphi.29 terminal protein, p3, essentially pure, was isolated in a denatured form from viral particles and anti-p3 antiserum was obtained. A radioimmunoassay to detect and quantitate protein p3 was developed. By using this assay, native protein p3 was highly purified from Escherichia coli cells harboring a gene 3-containing recombinant plasmid. After 3 purification steps, the protein was > 96% pure; its amino acid composition was very similar to that deduced from the nucleotide sequence of gene 3. The purified protein was active in the formation of the covalent p3-dAMP initiation complex when supplemented with extracts of B. subtilis infected with a sus mutant of .vphi.29 in gene 3. No DNA polymerase or ATPase activities were present in the final preparation of protein p3.This publication has 47 references indexed in Scilit:
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