作者: A.R. Poole , A. Reiner , L.H. Tang , L. Rosenberg
DOI: 10.1016/S0021-9258(19)70561-4
关键词: Affinity chromatography 、 Type II collagen 、 Molecular biology 、 Monomer 、 Immunodiffusion 、 Hyaluronic Acid Binding 、 Immunoelectrophoresis 、 Antiserum 、 Proteoglycan 、 Biochemistry 、 Chemistry
摘要: Abstract Antisera have been prepared against purified proteoglycan monomer and link protein from bovine cartilages. The immunological properties of these species studied by immunodiffusion, Laurell rocket immunoelectrophoresis, crossed hemagglutination, immunofluorescence. raised either adult articular or foetal epiphyseal were monospecific. They did not react with protein, type II collagen, nor any other molecular isolated to nasal cartilage dissociative density gradient centrifugation followed chromatography under conditions on Sephacryl S-200, showed no reaction immunodiffusion. However, antisera a weak native immunoelectrophoresis (not detectable when chondroitinase ABC-treated was used), hemagglutination assay. These traces antibody inactivated immunoreaction in solution provide monospecific antiserum protein. Purified antibodies specific for monomer, some which the hyaluronic acid binding region anti-link sera affinity using monomer. contains 48,000- 44,000-dalton subunits, two immunologically distinguishable species. An immunoassay developed electrophoresis. A micro-method, crossed-immunoelectrophoresis, studying hyaluronate is described. complex bound dissociated antibody.