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- W1991237581 abstract "Vitronectin (VN) is a cell attachment glycoprotein present in plasma and the extracellular matrix that also has multiple regulatory roles in the complement, coagulation, and fibrinolytic systems. VN stabilizes plasminogen activator inhibitor-1 (PAI-1) with potential binding sites reported at both the somatomedin B and heparin binding domains. In order to perform detailed structure-function analyses of VN, we have produced and expressed a recombinant baculovirus containing the cDNA of human VN. Recombinant VN (rVN) was secreted as a single chain 70-kDa protein into the serum-free culture medium of infected Spodoptera frugiperda cells. Maximum rVN levels of 33.9 mg/liter were obtained 48 hours post-infection. Purification of rVN from serum-free medium was achieved with single-step anion-exchange chromatography. Several native post-translational modifications were demonstrated in rVN including the presence of N-linked oligosaccharides, tyrosine sulfation, and serine phosphorylation. Recombinant VN retained cell and PAI-1 binding capacity. Therefore, rVN expressed for the first time in insect cells retains many post-translational modifications and functional activities and will be useful for additional structure-function analyses." @default.
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- W1991237581 date "1993-08-01" @default.
- W1991237581 modified "2023-09-24" @default.
- W1991237581 title "Expression of a Recombinant Baculovirus for Vitronectin in Insect Cells: Purification, Characterization of Post-translational Modifications and Functional Studies of the Recombinant Protein" @default.
- W1991237581 doi "https://doi.org/10.1006/abbi.1993.1372" @default.
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