Enzymatic fragmentation of cation exchange membrane bound immunoglobulin G.
Immunoglobulin G (IgG) was immobilized on a stack of microporous cation-exchange membranes and pulsed with pepsin solution. Fc fragment and its sub-fragments thus produced were removed along with the reaction flow-through, whereas F(ab')(2) which remained membrane bound could subsequently be eluted in a pure form using salt. The extent of IgG fragmentation and the apparent reaction rate constant were both significantly higher than in equivalent liquid phase reaction, presumably due to a combination of mass transport, steric, and substrate concentration effects. This approach of using a membrane surface as molecule cutting board could be attractive in niche applications such as integrated enzymatic reaction and purification processes involving macromolecular substrates.
Dept. of Chemical Engineering, McMaster University, Hamilton, ON, Canada L8S 4L7.
Deqiang
D
Yu
Raja
R
Ghosh
D015153:Blotting, Western; D002411:Cation Exchange Resins; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007074:Immunoglobulin G / Q000378:metabolism*; D008567:Membranes, Artificial
D002411:Cation Exchange Resins; D007074:Immunoglobulin G; D008567:Membranes, Artificial