ISSN:
1612-1112
Keywords:
Affinity chromatography
;
Biorecognition
;
Proteins
;
Polyacrylamide gels
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Summary Acrylamide and N,N′-methylenebisacrylamide were copolymerized in the presence of a protein to form a gel which was pressed through a sieve. The gel particles obtained were packed into a chromatographic tube. The experimental conditions for the polymerization are such that the pores of the gel particles are large enough to permit the protein to diffuse out of the particles, so that the entrapped protein can be removed from the bed by washing with an aqueous solution. However the interaction with the matrix is so strong that the protein can be desorbed only by a buffer containing 0.5 M sodium chloride or by a 10% solution of acetic acid containing 10% SDS. When a sample containing the protein present during the polymerization was applied to the column along with other proteins this protein was the only one adsorbed. The technique worked selectively with hemoglobin, cytochrome C and transferrin.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02290306
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