Premium
Synthesis and characterization of an acrylamide‐based water‐soluble affinity polymer for trypsin purification
Author(s) -
Sigmundsson Kristmundur,
Filippusson Hör∂ur
Publication year - 1996
Publication title -
polymer international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.592
H-Index - 105
eISSN - 1097-0126
pISSN - 0959-8103
DOI - 10.1002/(sici)1097-0126(199612)41:4<355::aid-pi624>3.0.co;2-3
Subject(s) - ultrafiltration (renal) , trypsin , chemistry , acrylamide , polymer , membrane , chymotrypsin , chromatography , polymer chemistry , molecular mass , copolymer , enzyme , organic chemistry , biochemistry
An acrylic polymer capable of specifically binding the enzyme trypsin has been synthesized by the copolymerization of acrylamide and N ‐acryloyl‐ m ‐aminobenzamidine. The object of the study was to discover suitable conditions for the synthesis of an affinity polymer which could be used in an ultrafiltration system for the biospecific affinity isolation of trypsin from mixtures containing other proteins. The polymer was purified by washing in an ultrafiltration system using a membrane with nominal molecular cutoff of 300 000. The molecular weight of the polymer product was varied by varying the concentration of initiator. The products were studied by nuclear magnetic resonance spectroscopy, by infrared spectroscopy, by viscometry and by their ability to inhibit trypsin in the absence and presence of ammonium sulphate at concentrations commonly found in crude protein solutions. No inhibition towards chymotrypsin activity was detected.