title: A simple method for affinity purification of radiolabeled monoclonal antibodies.
abstract: A simple method is described for affinity purification of radiolabeled antibodies using glutaraldehyde-fixed tumor target cells. The cell-bound antibody fraction is removed from the cells by an acid wash and then immediately subjected to buffer-exchange chromatography. The method was applied to the D3 murine monoclonal antibody which binds to a 290 kDa antigen on the surface of Line 10 guinea pig carcinoma cells. No alteration in the molecular size profile was detected after acid washing. Purification resulted in a significant increase in immunoreactivity by an average of 14 +/- 47% (SD; range 4-30%).
authors: Department of Nuclear Medicine, National Cancer Institute, NIH, Bethesda, MD 20892.
authors: M
authors: M
authors: Juweid
authors: J
authors: J
authors: Sato
authors: C
authors: C
authors: Paik
authors: S
authors: S
authors: Onay-Basaran
authors: J N
authors: JN
authors: Weinstein
authors: R D
authors: RD
authors: Neumann
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology / Q000302:isolation & purification*; D000915:Antibody Affinity; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D005976:Glutaral; D006168:Guinea Pigs; D007457:Iodine Radioisotopes; D051379:Mice; D016707:Tissue Fixation; D014407:Tumor Cells, Cultured / Q000276:immunology
chemical_list: D000911:Antibodies, Monoclonal; D007457:Iodine Radioisotopes; D005976:Glutaral