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Title: Synthesis and processing in Escherichia coli of human leucocyte interferon fused with the signal sequence of Bacillus amyloliquefaciens a-amylase

Journal Article · · Dokl. Biol. Sci. (Engl. Transl.); (United States)
OSTI ID:5629013

Earlier, the authors reported cloning of the alpha-amylase gene of B. amyloliquefaciens in B. subtilis and E. coli. Currently, the authors report results on the expression of the hybrid gene consisting of the DNA fragment coding for the leader part of B. amyloliquefaciens alpha-amylase and the structural part of the human interferon alpha-2 in E. coli cells. This gene contains an additional methionine codon at the 5'-terminal, which codes for the interferon structure (without its own signal peptide). The interferon gene was inserted into plasmid /sub p/TG 278 at the cleavage site of EcoRI. The structure of the plasmid thus obtained the signal peptide of amylase, five amino acids (Val-Gly-Glu-Phe-Met), and the structural part of the interferon. The E. coli C600 cells carrying plasmid pTGA6 were used to study interferon secretions. The interferon activity was determined radioimmunologically with the use of monoclonal anti-bodies NK2.

Research Organization:
All-Union Scientific-Research Institute of Genetics and Breeding of Industrial Microorganisms, Moscow, USSR
OSTI ID:
5629013
Journal Information:
Dokl. Biol. Sci. (Engl. Transl.); (United States), Vol. 282:1-6; Other Information: Translated from Dokl. Akad. Nauk SSSR; 282: No. 2, 1490-1493(Jun 1985)
Country of Publication:
United States
Language:
English

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