Selective removal of plasma components by high-performance immunoaffinity chromatography.
Affinity chromatography employing immobilized antibody is a rapid and specific technique for isolating biologically active materials from different sources, and high-performance immunoaffinity chromatography (HPIAC) has been used to isolate antibodies and antigens for medical application. In an attempt to resolve the problem of amyloid deposition in dialysis patients, we used HPIAC to specifically remove beta2-microglobulin from human plasma. The use of a membrane as an affinity ligand support was also studied. The specific antibody immobilized on a membrane was highly effective for removal of rat immunoglobulin E passed through an extracorporeal circulation system (ECS). Then we investigated the removal of injected human serum amyloid P component from the blood of rats by means of the ECS. Biocompatibility of the specific antibody-bearing immunoaffinity membrane was also examined in terms of nonspecific binding of other plasma components. These techniques should prove useful for medical application and may have broad applicability for the elimination of any unwanted plasma component.
Kojima
K
K
Hatano Research Institute, Food and Drug Safety Center, Kanagawa, Japan.
D000818:Animals; D001798:Blood Proteins / Q000302:isolation & purification*; D002846:Chromatography, Affinity / Q000379:methods*; D005112:Extracorporeal Circulation; D006801:Humans; D007073:Immunoglobulin E / Q000302:isolation & purification; D008567:Membranes, Artificial; D010956:Plasmapheresis / Q000379:methods*; D051381:Rats; D000683:Serum Amyloid P-Component / Q000302:isolation & purification; D001613:beta 2-Microglobulin / Q000302:isolation & purification
D001798:Blood Proteins; D008567:Membranes, Artificial; D000683:Serum Amyloid P-Component; D001613:beta 2-Microglobulin; D007073:Immunoglobulin E