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  4. Structure of hu.-rec. IFN gamma
 
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1989
Journal Article
Title

Structure of hu.-rec. IFN gamma

Abstract
Hu-IFN-gamma (143aa) was shortened by recombinant methods at the NH2-terminus by 1, 3 and 8 and at the COOH-end by 10, 11, 14 and 19aa. These mutants were expressed in bacterial cells, purified to more than 90 per cent and analysed in respect to molecular structure: dimer versus monomer and to antiviral activity. Loss of aa at the NH2-terminus conserves the dimeric structure whereas a shortage of 14 or 19 aa at the COOH-end results in a monomeric organisation. In contrast to all other mutants the two latter ones do not precipitate at high expression rates. Mutants shortened at the COOH-end by up to 11 aa even increase antiviral activity; a further additional take off by 3 or more aa drastically reduces activity. At the NH2-terminus the first 3 aa are not important for activity; a further shortage affects activity as well as a non precipitating monoclonal antibody, which recognizes the first 6 aa does neutralize antiviral activity. Mutants lacking 3 aa at the NH2-terminus or 11 at the C OOH-end, which both alone are fully active, show, combined in a double mutant, a 30 fold decrease in activity; this double mutant indicate and interaction of the ends of the protein for activity which may be important too for the structure.
Author(s)
Boehm, J.
Otto, B.
Schöne, B.
Slodowski, O.
Journal
Journal of Interferon Research  
Conference
Meeting on the Interferon System 1989  
Language
English
ITA  
Keyword(s)
  • genetic technology

  • interferon gamma

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