A chromatographic process based on monoliths for purification of infective baculovirus without prior concentration step has been established. Baculovirus produced in Spodoptera frugiperda cells (Sf-9) were harvested by centrifugation, filtered through 0.8 μm filters and directly loaded onto radial 1 mL anion exchange monoliths with a channel size of 1.
View Article and Find Full Text PDFPeptides as therapeutic substances are efficient agents in the treatment of several diseases. However, they often have to be chemically modified in order to be suited as therapeutic agent. Conjugation to large carrier molecules is often required.
View Article and Find Full Text PDFEpitope mapping using antibodies against factor VIII (FVIII) has been performed using blotting techniques with truncated and/or digested FVIII molecules. Here, we focused on the precise mapping of affinity purified IgG from patients with an immune response against blood clotting FVIII using synthetic peptide arrays on cellulose membranes comprising the entire sequence of FVIII. The aim was to elucidate the epitope profile from different inhibitors and possibly detect new epitopes, which have not been described before.
View Article and Find Full Text PDFThe development of antibodies against blood clotting factor VIII is a major complication affecting 20-30% of hemophilia A patients receiving replacement with FVIII concentrates. This study investigated generating peptides acting as broadly neutralizing agents to block factor VIII antibodies. These peptides were selected from dual positional scanning decapeptide libraries on cellulose membranes.
View Article and Find Full Text PDFThe methylotrophic yeast Pichia pastoris is often used as an organism for the heterologous expression of proteins and has been used already for production of a number of glycosyltransferases involved in the biosynthesis of N- and O-linked oligosaccharides. In our recent studies, we have examined the expression in P. pastoris of Arabidopsis thaliana and Drosophila melanogaster core alpha1,3-fucosyltransferases (EC 2.
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