Production and properties of a bifunctional fusion protein that mediates attachment of vero cells to cellulosic matrices |
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Authors: | Wierzba A Reichl U Turner R F Warren R A Kilburn D G |
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Institution: | Biotechnology Laboratory and Department of Chemical Engineering, The University of British Columbia, 237-6174 University Boulevard, Vancouver, British Columbia, V6T 1Z3, Canada. |
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Abstract: | The sequence Arg-Gly-Asp (RGD) in extracellular matrix proteins such as fibronectin, collagen, and laminin mediates cell attachment by interacting with proteins of the integrin family of cell surface receptors. A gene fusion encoding the RGD-containing peptide, fused to the C-terminus of a cellulose-binding domain (CBD/RGD), was expressed in Escherichia coli. Cultures produced up to 50 mg of CBD/RGD per liter, most of which was extracellular. It was purified from the culture supernatant by affinity chromatography on cellulose. CBD/RGD promoted the attachment of green monkey Vero cells to polystyrene and cellulose acetate. Attachment was inhibited by small synthetic peptides containing the RGD sequence. CBD/RGD was as effective as collagen in promoting the attachment of Vero cells to Cellsnowtrade mark microcarriers. (c) 1995 John Wiley & Sons, Inc. |
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Keywords: | arg-gly-asp cellulose protein production |
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