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Construction and phosphorylation of a fusion protein Hu-IFN-alpha A/gamma

Zhao, X X ; Li, B L ; Langer, J A ; Van Riper, G ; Pestka, S

Analytical biochemistry, 01 May 1989, Vol.178(2), pp.342-7 [Peer Reviewed Journal]

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  • Title:
    Construction and phosphorylation of a fusion protein Hu-IFN-alpha A/gamma
  • Author: Zhao, X X ; Li, B L ; Langer, J A ; Van Riper, G ; Pestka, S
  • Description: A protein consisting of human (Hu)-IFN-alpha A to which the COOH-terminal 16 amino acids of Hu-IFN-gamma were fused was prepared by constructing an expression vector by oligonucleotide-directed mutagenesis. The hybrid protein Hu-IFN-alpha A/gamma was expressed under the control of phage lambda PL promoter. The protein was purified with the use of a monoclonal antibody against Hu-IFN-alpha or the COOH-terminal amino acid sequence of Hu-IFN-gamma. The purified protein exhibited a single major band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and has antiviral activity on human and bovine cells. Unlike Hu-IFN-alpha A, but similar to Hu-IFN-gamma, the hybrid Hu-IFN-alpha A/gamma can be phosphorylated by [gamma 32P]ATP and cAMP-dependent protein kinase. The phosphorylated molecule binds to the IFN-alpha/beta receptor. The introduction of a phosphorylation site into Hu-IFN-alpha A by fusion of the region of Hu-IFN-gamma which contains the phosphorylation site provides a new reagent for studies of receptor binding, pharmacokinetics, and other studies where labeled interferons are useful. Furthermore, the introduction of phosphorylation sites into proteins provides a new principle for the preparation of a wide variety of reagents for many purposes.
  • Is Part Of: Analytical biochemistry, 01 May 1989, Vol.178(2), pp.342-7
  • Identifier: ISSN: 0003-2697 ; PMID: 2502045 Version:1
  • Subjects: Interferon Type I ; Interferon-Gamma ; Recombinant Fusion Proteins ; Recombinant Proteins
  • Language: English

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