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Immobilized iminodiacetic acid (IDA)‐type Cu 2+ ‐chelating membrane affinity chromatography for purification of bovine liver catalase
Author(s) -
Yang Li,
Jia Lingyun,
Zou Hanfa,
Zhang Yukui
Publication year - 1999
Publication title -
biomedical chromatography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.4
H-Index - 65
eISSN - 1099-0801
pISSN - 0269-3879
DOI - 10.1002/(sici)1099-0801(199905)13:3<229::aid-bmc825>3.0.co;2-i
Subject(s) - chemistry , iminodiacetic acid , chelation , chromatography , membrane , adsorption , imidazole , copper , affinity chromatography , metal ions in aqueous solution , cellulose , nuclear chemistry , metal , enzyme , inorganic chemistry , biochemistry , organic chemistry
A metal ion chelating membrane medium based on iminodiacetate‐substituted modified short cotton cellulose was examined for the purification of bovine liver catalase (BLC). The effect of buffer pH, chelator surface density, initial concentration of crude enzyme and flow rate on BLC binding efficiency to the copper ion chelating membrane adsorbent were examined. Under the chromatographic conditions chosen, 67.7% recovery of BLC was attained with an overall 4.2‐fold increase in specific activity in a single step. After performance of BLC purification, the chelating membrane adsorbent can be easily regenerated by imidazole or EDTA buffer with higher reviving effectiveness with the latter. Copyright © 1999 John Wiley & Sons, Ltd.