Comparison of L-tryptophan binding capacity of BSA captured by a polymer brush with that of BSA adsorbed onto a gel network.
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.
Ito
H
H
Department of Materials Technology, Faculty of Engineering, Chiba University, Inage, Japan.
Nakamura
M
M
Saito
K
K
Sugita
K
K
Sugo
T
T
D000818:Animals; D000837:Anion Exchange Resins; D002417:Cattle; D011108:Polymers; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D014364:Tryptophan / Q000378:metabolism*
D000837:Anion Exchange Resins; D011108:Polymers; D012710:Serum Albumin, Bovine; D014364:Tryptophan