Further characterization of carboxymethylated aspartic acid agarose. Purification of human alpha 2-macroglobulin and hemopexin

Autor:	T, Mantovaara, H, Pertoft, J, Porath
Rok vydání:	1991
Předmět:	Aspartic Acid Hemopexin Sepharose Animals Humans Cattle Electrophoresis Polyacrylamide Gel alpha-Macroglobulins Cobalt Chromatography Affinity
Zdroj:	Biotechnology and applied biochemistry. 13(3)
ISSN:	0885-4513
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::d3fc8180f988dbe5d670c7166dda726a https://pubmed.ncbi.nlm.nih.gov/1715716 Zobrazit plný text záznamu Plný text