title: Protein adsorption to hydrophobic Zeolite Y: salt effects and application to protein fractionation.
abstract: The binding equilibria of proteins with a hydrophobic variety of crystalline Zeolite Y is affected by salt and is a function of the type of salt and its concentration. The behaviour does not always follow the conventional pattern of increased binding at high salt concentrations and varies also for the different proteins involved. The overall process may be looked upon as a salting-in/salting-out mechanism. This material can be used as a surface for the selective adsorption of proteins and has been applied for the fractionation of ox heart homogenate in multi-stage operations. The presence of NaCl influences the protein binding, and this can be seen by monitoring the activity profile of lactate dehydrogenase. The bound protein can be reversed by treating the equilibrium mixture with low-molecular-mass poly(ethylene glycol)s.
authors.affiliation: Department of Biotechnology, Lund University, Sweden.
authors.forename: S
authors.initials: S
authors.lastname: Ghose
authors.forename: B
authors.initials: B
authors.lastname: Mattiasson
mesh_terms: D000327:Adsorption; D000645:Ammonium Sulfate / Q000737:chemistry; D000818:Animals; D002417:Cattle; D005591:Chemical Fractionation; D006321:Heart; D007074:Immunoglobulin G / Q000737:chemistry / Q000302:isolation & purification; D008297:Male; D008970:Molecular Weight; D009113:Muramidase / Q000737:chemistry / Q000302:isolation & purification; D011092:Polyethylene Glycols / Q000737:chemistry; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000302:isolation & purification; D014020:Tissue Extracts; D017641:Zeolites / Q000737:chemistry*
chemical_list: D007074:Immunoglobulin G; D011506:Proteins; D014020:Tissue Extracts; D017641:Zeolites; D012710:Serum Albumin, Bovine; D011092:Polyethylene Glycols; D009113:Muramidase; D000645:Ammonium Sulfate