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  • Title: Production of biologically active recombinant avidin in baculovirus-infected insect cells.
    Author: Airenne KJ, Oker-Blom C, Marjomäki VS, Bayer EA, Wilchek M, Kulomaa MS.
    Journal: Protein Expr Purif; 1997 Feb; 9(1):100-8. PubMed ID: 9116491.
    Abstract:
    An efficient lepidopteran insect cell system was established for the expression of a recombinant form of chicken egg-white avidin. The gene product was obtained in both secreted and intracellular forms, and biologically active recombinant avidin was isolated using affinity chromatography on an iminobiotin-agarose column. Similar to the known quaternary structure of the native egg-white protein, the purified recombinant protein was glycosylated and assembled mainly into tetramers. Like native avidin, the recombinant tetramer also exhibited a high level of thermostability, and was further stabilized upon binding biotin. The biotin-binding and structural properties of the recombinant avidin are thus similar to those of the natural egg-white protein, and the insect system is appropriate both for future site-directed mutagenesis studies and for the production of avidin fusion proteins.
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