Protein A, hydroxyapatite and diethylaminoethyl: evaluation of three procedures for the preparative purification of monoclonal antibodies by high-performance liquid chromatography.
Three rapid, reproducible and feasible monoclonal antibody purification procedures by means of high-performance liquid chromatography have been evaluated. The stationary phases employed were high-performance hydroxyapatite, high-performance Protein A and high-performance anion-exchange resin. The purity of the final immunoglobulin preparations was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions and, subsequently, by high-performance gel permeation chromatography. The immunoreactivity of purified monoclonal antibodies was determined by the radioimmunoassay method.
Poiesi
C
C
Department of Clinical Chemistry and Propedeutic Biochemistry, University of Brescia, Italy.
Tamanini
A
A
Ghielmi
S
S
Albertini
A
A
D000818:Animals; D000911:Antibodies, Monoclonal / Q000302:isolation & purification*; D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006882:Hydroxyapatites; D051379:Mice; D013205:Staphylococcal Protein A
D000911:Antibodies, Monoclonal; D006882:Hydroxyapatites; D013205:Staphylococcal Protein A