Co-autodisplay of Z-domains and bovine caseins on the outer membrane of E. coli
- Co-autodisplay of Z-domains and bovine caseins on the outer membrane of E. coli
- 유구; Thorsten Saenger; 봉지홍; Joachim Jose; 강민정; 변재철
- Autodisplay; Z-domain; Casein; FACS; Immunoassay
- Issue Date
- Biochimica et biophysica acta, Biomembranes
- VOL 1848, NO 12, 3126-3133
- In this work, two proteins, Z-domains and bovine casein, were autodisplayed on the outer membrane of the same Escherichia coli cells by co-transformation of two different autodisplay vectors. On the basis of SDS-PAGE densitometry, Z-domains and bovine casein were expressed at 3.12 × 105 and 1.55 × 105 proteins/E. coli cell, respectively. The co-autodisplayed Z-domains had antibody-binding activity and the bovine casein had adhesive properties. E. coli with co-autodisplayed proteins were analyzed by fluorescence assisted cell sorting (FACS). E. coli with co-autodisplayed Z-domains and bovine casein aggregated due to hydrophobic interaction. For application to immunoassays, the Z-domain activity was estimated after (1) immobilizing the E. coli and (2) forming an OM layer. E. coli with co-autodisplayed two proteins that were immobilized on a polystyrene microplate had
the same antibody-binding activity as did E. coli with autodisplayed Z-domains only. The OM layer from the cotransformed E. coli had Z-domains and bovine casein expressed at a 1:2 ratio from antibody-binding activity measurements.
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