The IFN-alpha-inducing capacity of Sendai Virus in human leukocytes is independent from the hemagglutinating and hemolytic activities and from the viral proteins of the Sendai Virus preparations.

About 30 Sendai Virus (SV) preparations, examined for their capacity to induce natural human interferon alpha from fresh human leukocytes (Le-IFN-alpha) of healthy donors, were characterized for hemagglutinating (HA) and hemolytic (HemA) activities and for SDS-PAGE proteic pattern. The SV preparations were produced by a single passage or by serial propagations through eggs in different conditions of multiplicity of infection (m.o.

Antigenic characterization of recombinant, lymphoblastoid, and leukocyte IFN-alpha by monoclonal antibodies.

To gain more insight into similarities of different interferon-alpha (IFN-alpha) species, we evaluated neutralization and immunoactivity of a variety of IFN preparations with various monoclonal antibodies (IFN-alpha mAb). Nine IFN-alpha mAb obtained through immunization with recombinant IFN-alpha (rmAb), lymphoblastoid IFN-alpha (LY mAb), and leukocyte IFN-alpha (LE mAb) were tested. The IFN-alpha mAb were evaluated for their ability to neutralize the antiviral activity of 11 recombinant IFN-alpha subtypes, two recombinant IFN-alpha hybrids, and lymphoblastoid and leukocyte IFN-alpha preparations.

Capillary electrophoresis of heparin and dermatan sulfate unsaturated disaccharides with triethylamine and acetonitrile as electrolyte additives.

Capillary electrophoresis at constant voltage with the addition of triethylamine as electrolyte to a running buffer containing borate using fused-silica capillaries permits the complete resolution in less than 30 min of 11 standard heparin and 8 standard dermatan sulfate disaccharides, which represent degradation products of heparin and dermatan sulfate by specific lyases. Triethylamine influences the migration time of disaccharides by reducing both their electrophoretic mobility towards the anode and the electroosmotic flow towards the cathode. A modulated combination of these effects together with borate-disaccharide complex formation is responsible for separation, especially in the case of isomers which differ in the position of the sulfate groups.

Purification of recombinant human interferon-beta by immobilized antisense peptides.

Synthetic antisense peptides encoded in the antisense strands of DNA corresponding to the 1-14, 42-54 and 103-115 fragments of the human interferon-beta sequence were applied in the purification of recombinant human interferon-beta from a mammalian cell culture. The protein fragments were selected on the basis of their computer-predicted exposure on the surface of the protein. The antisense peptides were synthetized by the solid-phase method directly on the resin used as the stationary phase in affinity chromatography.