Immunochemical properties of human low density lipoproteins as explored by monoclonal antibodies. Binding characteristics distinct from those of conventional serum antibodies.

摘要: Abstract Spleen cells obtained from mice immunized with human plasma low-density lipoproteins (LDL) were fused mouse myeloma cells. The resulting hybridoma secreting immunoglobulin specific for LDL screened and scored by radioimmunoassay cloned multiple limiting dilutions. Immunochemical properties of the monoclonal antibodies compared convential serum antibodies. It was found that conventional precipitated bound more than 95% 125 I-labeled maximal binding independent temperature. incapable precipitating a maximum only 20% total LDL. between extremely temperature-dependent. An optimal degree observed at 4°C, whereas 37°C 30% achieved 4°C. Although low, could be re-established following subsequent incubation suggesting antigenic structure is reversibly modulated temperatures 4 37°C. Since orientation apolipoprotein B in known to dynamic different temperatures, this result suggests antibodies, but not are capable detecting subtle conformational changes In addition, we have determined affinity Only showed linear Scatchard plot, single site affinity. also possessed high specificity failed react porcine LDL, while recognize both