No abstract

A recombinant antigen (p22-NS3), possessing putative HCV nucleocapsid protein (~22) and non-structural protein 3 (NS3) epitopes, was heavily expressed m E. co11 and purified. The p22-NS3 purified recombmant antigen strongly reacts with sera containing human antibodies directed against p22 and NS3 providing a starting point for the design of an HCV single all-encompassmg antigen for a blood screening assay.

The enzyme L-asparaginase was covalently immobilized on the inner surface of the hollow fibers utilized in a commercially available dialyzer by the periodate method. After sterilization with gamma radiation the bioreactor was able to metabolize in vivo, 90 per cent of circulating asparagine in two hours. The absence in blood of asparaginase-related protein fragments, released from the hollow fiber immobilized enzyme, was monitored using a specific enzyme-linked immunosorbent assay (ELISA).