[Expression in Escherichia coli of the human leukocyte interferon alpha2 gene fused with N-terminal fragment of beta-galactosidase].
Genes for leucocyte interferon and alpha-donor of galactosidase were fused by deletion mutagenesis or by site-directed mutagenesis. In both cases the fused protein was expressed. The protein having an antiviral activity of leucocyte interferon was easily detected in bacteria and solutions by the reaction of beta-galactosidase alpha-complementation and retained the antigenic determinants of interferon and beta-galactosidase. The use of fused proteins for optimization of gene expression and for the analysis of interferon structure-function relationship is discussed.
D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics*; D005696:Galactosidases / Q000235:genetics*; D005786:Gene Expression Regulation; D006801:Humans; D007370:Interferon Type I / Q000235:genetics*; D014176:Protein Biosynthesis; D011994:Recombinant Proteins / Q000235:genetics; D001616:beta-Galactosidase / Q000235:genetics*
D007370:Interferon Type I; D011994:Recombinant Proteins; D005696:Galactosidases; D001616:beta-Galactosidase
Ekspressiia v Escherichia coli gena leĭkotsitarnogo alpha2-interferona cheloveka, transliatsionno slitogo s N-kontsevym fragmentom beta-galaktozidazy.