Protein adsorption characteristics of porous and tentacle anion-exchange membrane prepared by radiation-induced graft polymerization

Satoshi Tsuneda, Kyoichi Saito*, Takanobu Sugo, Keizo Makuuchi

*この研究の対応する著者

研究成果: Article査読

49 被引用数 (Scopus)

抄録

A polymer chain containing a diethylamino group was grafted onto the pore surface of a porous hollow-fiber membrane by radiation-induced graft polymerization. Dependence of the protein binding capacity of the membrane on environmental parameters such as salt concentration, pH and temperature was investigated. Saturation capacity of protein bound onto the graft chain containing ion-exchange group was governed by the conformation of the graft chain and the intensity of ion-exchange interaction. The conformation of the graft chain was investigated based on the pore radius of the membrane estimated from the permeation flux of a buffer solution through the membrane. By sufficiently permeating a bovine serum albumin (BSA) solution within the concentration range of 0.2-10 mg-BSA/ml through the membrane, the BSA binding capacity was determined. With increasing salt concentration or pH of the protein buffer solution, the graft chain shrank and BSA binding capacity decreased. On the other hand, the BSA binding capacity slightly increased with increasing temperature, and the conformation of the graft chain was insensitive to temperature in the range from 278 to 303 K. The bound BSA could be quantitatively eluted by permeating a buffer solution containing 0.5 M NaCl, and no deterioration in the BSA binding capacity was observed during five cycles of adsorption, elution and conditioning.

本文言語English
ページ(範囲)239-245
ページ数7
ジャーナルRadiation Physics and Chemistry
46
2
DOI
出版ステータスPublished - 1995 8
外部発表はい

ASJC Scopus subject areas

  • 放射線

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