Expression in E. coli and purification of a chimeric p22-NS3 recombinant antigen of hepatitis C virus (HCV).

A recombinant antigen (p22-NS3), possessing putative HCV nucleocapsid protein (p22) and non-structural protein 3 (NS3) epitopes, was heavily expressed in E. coli and purified. The p22-NS3 purified recombinant 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-encompassing antigen for a blood screening assay.

Hollow fiber immobilized L-asparaginase: in vivo and in vitro immunological studies.

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).

[Immobilization of antibodies against Australia antigen on nylon spheres: use in immunoenzymatic determination of HBsAg].

Antibodies against HBsAg were immobilized by covalent linkage on nylon beads to be used in solid phase enzyme-linked immunoassays. The covalent bond between the protein and the partially hydrolyzed support was obtained via glutaraldehyde or succinylester methods. These particular solid phases were compared, in a conventional enzyme-linked immunosorbent assay for hepatitis B antigen, with polystyrene beads coated by simple adsorption of IgG on plastic surface.