title: Purification and properties of non-precipitating antibodies to cobrotoxin.
abstract: The heterogeneity of precipitating and non-precipitating antibodies to cobrotoxin was demonstrated by their elution pattern on cobrotoxin-Sepharose and chromatography on DEAE-cellulose column. Gel filtration patterns on a Sepharose 6B column revealed that the soluble complexes formed from non-precipitating antibody and HNB-cobrotoxin at a different molar ratio all emerged in the void volume, indicating that the molecular weight of the soluble complex is around 4,000,000 or larger. Unreacted free non-precipitating antibody coincided with the peak of IgG and was proved to be free from HNB-cobrotoxin. The molar ratio of antibody to antigen for the soluble complex was found to be 0.79 to 0.97 indicating that 1.58--1.94 molecules of non-precipitating antibody are bound to HNB-cobrotoxin instead of three molecules as in the case of precipitating antibody.
mesh_terms: D000906:Antibodies / Q000302:isolation & purification*; D000936:Antigen-Antibody Complex; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003039:Cobra Neurotoxin Proteins / Q000276:immunology*; D004546:Elapid Venoms / Q000276:immunology*; D007140:Immunoglobulin Fab Fragments / Q000302:isolation & purification; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification
chemical_list: D000906:Antibodies; D000936:Antigen-Antibody Complex; D003039:Cobra Neurotoxin Proteins; D004546:Elapid Venoms; D007140:Immunoglobulin Fab Fragments; D010446:Peptide Fragments