Purification in a functional form of the terminal protein of Bacillus subtilis phage phi 29.

Abstract:

:Phage phi 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 three purification steps, the protein was more than 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 phi 29 in gene 3. No DNA polymerase or ATPase activities were present in the final preparation of protein p3.

authors

Prieto I,Lázaro JM,García JA,Hermoso JM,Salas M

doi

10.1073/pnas.81.6.1639

subject

Has Abstract

pub_date

1984-03-01 00:00:00

pages

1639-43

issue

6

eissn

0027-8424

issn

1091-6490

journal_volume

81

pub_type

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