Selective removal of chymotrypsin using diphenyl alpha-aminoalkylphosphonate immobilized on sepharose gel.
A diphenyl alpha-aminoalkylphosphonate derivative, which is an irreversible inhibitor of chymotrypsin-like serine proteases, was immobilized on cyanogen bromide-activated Sepharose, and the selective binding of chymotrypsin to the obtained inhibitor-gel was evaluated using batch and column methods. Complete removal of chymotrypsin in an aqueous solution was done using the column method, while partial removal was done using the batch method.
Ono
Shin
S
Department of System Engineering of Materials and Life Science, Faculty of Engineering, Toyama University, Japan. shinono@eng.toyama-u.ac.jp
Umezaki
Makiko
M
Nabari
Hajime
H
Nakayama
Ryutaro
R
Hasegawa
Kumi
K
Sako
Satomi
S
Fujii
Takayoshi
T
Yamazaki
Isao
I
Yoshimura
Toshiaki
T
D002918:Chymotrypsin / Q000737:chemistry / Q000302:isolation & purification*; D063065:Organophosphonates / Q000737:chemistry*; D012685:Sepharose / Q000737:chemistry*
D063065:Organophosphonates; D012685:Sepharose; D002918:Chymotrypsin