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Site-Specific, Enzymatic Biotinylation of Recombinant Proteins in Spodoptera Frugiperda Cells Using Biotin Acceptor Peptides

  1. Author:
    Duffy, S.
    Tsao, K. L.
    Waugh, D. S.

  2. Author Address

    Waugh DS NCI ABL BASIC RES PROGRAM FREDERICK CANC RES & DEV CTR POB B FREDERICK, MD 21702 USA NCI ABL BASIC RES PROGRAM FREDERICK CANC RES & DEV CTR FREDERICK, MD 21702 USA HOFFMANN LA ROCHE INC ROCHE RES CTR NUTLEY, NJ 07110 USA
    1. Year: 1998
  2. Journal: Analytical Biochemistry
    1. 262
    2. 2
    3. Pages: 122-128
  4. Type of Article: Article
  1. Abstract:

    Site-specific, enzymatic biotinylation of recombinant proteins can be exploited to circumvent many problems associated with the use of biotinylating reagents in vitro and to overcome some of their inherent Limitations. Additionally, biotinyl proteins can be purified to near-homogeneity in a single step under native conditions. Here we report that a biotin acceptor peptide (BAP) substrate for Escherichia coil biotin holoenzyme synthetase (BirA) can be used to label recombinant proteins with biotin in Spodoptera frugiperda (Sf9) cells, and we describe a collection of baculovirus transfer vectors specifically designed for this purpose. These BioBac vectors will greatly expand the range of proteins to which this technology can be applied. (C) 1998 Academic Press. [References: 30]

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