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Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/38098
Title: Overproduction and purification of the connector protein of Bacillus subtilis phage ø29
Authors: Ibáñez Pérez, Carmen; García, Juan Antonio; Carrascosa, José L.; Salas, Margarita
Issue Date: 1984
Publisher: Oxford University Press
Citation: Nucleic Acids Research 12 (5): 2351-2365 (1984)
Abstract: A ø29 DNA fragment containing genes 10 and 11, coding for the connector protein and the lower collar protein, respectively, has been cloned in the pBR322 derivative plasmid pKC30 under the control of the PL promoter of phage lambda. Two polypeptides with the electrophoretic mobility of proteins pl0 and p11 were labelled with 35S-methionine after heat induction. The proteins were characterized as pl0 and p11 by radioimmunoassay and they represented about 10% and 7%, respectively, of the total E. coli protein after 4 hours of induction. These proteins represent less than 1% of the B. subtilis protein in ø29-infected cells. Protein pl0 has been highly purified from the E.coli cells carrying the recombinant plasmid. Antibodies raised against the purified protein p10 reacted with the connector protein produced in ø29-infected B. subtilis.
Publisher version (URL): http://dx.doi.org/10.1093/nar/12.5.2351
URI: http://hdl.handle.net/10261/38098
ISSN: 0305-1048
DOI: 10.1093/nar/12.5.2351
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