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Further characterization of carboxymethylated aspartic acid agarose. Purification of human alpha 2‐macroglobulin and hemopexin
Author(s) -
Mantovaara T.,
Pertoft H.,
Porath J.
Publication year - 1991
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1991.tb00159.x
Subject(s) - hemopexin , agarose , iminodiacetic acid , chemistry , alpha 2 macroglobulin , chromatography , aspartic acid , elution , macroglobulin , affinity chromatography , sepharose , adsorption , chelation , biochemistry , amino acid , enzyme , inorganic chemistry , organic chemistry , heme
alpha 2‐Macroglobulin and hemopexin were purified by affinity chromatography on a recently introduced chelating matrix, i.e., carboxymethylated aspartic acid agarose, coupled with cobalt(II). Adsorption was performed at neutral pH and the proteins were eluted by lowering the pH to 5.0. An alternative method for desorption as well as comparison with iminodiacetic acid agarose coupled with cobalt(II) is also described.