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.
Yu
Deqiang
D
Dept. of Chemical Engineering, McMaster University, Hamilton, ON, Canada L8S 4L7.
Ghosh
Raja
R
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