title: Comparison of L-tryptophan binding capacity of BSA captured by a polymer brush with that of BSA adsorbed onto a gel network.
abstract: A polymer brush containing a diethylamino group as an anion-exchange group was appended onto a polymer substrate by radiation-induced graft polymerization and subsequent chemical modifications. Bovine serum albumin as a chiral ligand for L-tryptophan was bound to the polymer brush at a density ranging from 17 to 150 g BSA/l. For comparison, BSA was adsorbed onto the gel network containing a diethylaminoethyl group. The molar binding ratio of L-tryptophan to BSA on the polymer brush was 1.7-fold higher than that to BSA on the gel network.
authors.affiliation: Department of Materials Technology, Faculty of Engineering, Chiba University, Inage, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Ito
authors.forename: M
authors.initials: M
authors.lastname: Nakamura
authors.forename: K
authors.initials: K
authors.lastname: Saito
authors.forename: K
authors.initials: K
authors.lastname: Sugita
authors.forename: T
authors.initials: T
authors.lastname: Sugo
mesh_terms: D000818:Animals; D000837:Anion Exchange Resins; D002417:Cattle; D011108:Polymers; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D014364:Tryptophan / Q000378:metabolism*
chemical_list: D000837:Anion Exchange Resins; D011108:Polymers; D012710:Serum Albumin, Bovine; D014364:Tryptophan