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Purification of factor VIII:c coagulant activity from rat liver nonparenchymal cell culture medium by immobilized metal ion affinity chromatography
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.tb00147.x
Subject(s) - agarose , affinity chromatography , chromatography , chemistry , ion chromatography , chelation , polyacrylamide , polyacrylamide gel electrophoresis , calcium , sepharose , gel electrophoresis , aspartic acid , biochemistry , amino acid , enzyme , organic chemistry , polymer chemistry
The purification of factor VIII:c coagulant activity on the basis of its affinity for calcium is described. For this purpose, use was made of a recently introduced chelating matrix, i.e., carboxymethylated aspartic acid agarose, coupled with calcium–thereby creating a gel with specificity comparable with biospecific affinity chromatography. In a single step factor VIII:c activity was purified from rat liver nonparenchymal cell culture medium with a purification factor of 85‐fold. The material exhibits a single band on polyacrylamide gel electrophoresis.