Further characterization of carboxymethylated aspartic acid agarose. Purification of human alpha 2-macroglobulin and hemopexin.
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.
Mantovaara
T
T
Institute of Biochemistry, Uppsala University, Sweden.
Pertoft
H
H
Porath
J
J
D000818:Animals; D001224:Aspartic Acid / Q000031:analogs & derivatives*; D002417:Cattle; D002846:Chromatography, Affinity / Q000379:methods*; D003035:Cobalt; D004591:Electrophoresis, Polyacrylamide Gel; D006466:Hemopexin / Q000302:isolation & purification*; D006801:Humans; D012685:Sepharose / Q000031:analogs & derivatives*; D000511:alpha-Macroglobulins / Q000302:isolation & purification*
D000511:alpha-Macroglobulins; C070802:carboxymethylaspartic acid agarose; D001224:Aspartic Acid; D003035:Cobalt; D012685:Sepharose; D006466:Hemopexin