Affinity chromatography on a hydrophobic matrix using a heterobifunctional ligand.
Affinity adsorption chromatographic purification using heterobifunctional ligands and a hydrophobic support is described. Soybean trypsin inhibitor was modified with a detergent, with the result that hydrophobic residues were attached to the inhibitor. On passage through an octyl-Sepharose column the inhibitor was bound to the support. The modified inhibitor was still able to bind trypsin either in free solution or after the inhibitor was bound by the support. This procedure forms the basis for a robust affinity purification technique that can be made very general.
Kaul
R
R
Department of Biotechnology, University of Lund, Sweden.
Olsson
U
U
Mattiasson
B
B
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D007457:Iodine Radioisotopes; D008024:Ligands; D011506:Proteins / Q000032:analysis; D012685:Sepharose / Q000031:analogs & derivatives; D012967:Sodium Dodecyl Sulfate; D014357:Trypsin / Q000302:isolation & purification / Q000378:metabolism; D014360:Trypsin Inhibitor, Kunitz Soybean / Q000302:isolation & purification*; D014361:Trypsin Inhibitors / Q000302:isolation & purification*
D007457:Iodine Radioisotopes; D008024:Ligands; D011506:Proteins; D014361:Trypsin Inhibitors; D012967:Sodium Dodecyl Sulfate; C035771:Sepharose CL 4B; D012685:Sepharose; D014360:Trypsin Inhibitor, Kunitz Soybean; D014357:Trypsin