Affinity-chromatographic purification of human alpha 2-antiplasmin.
A new simple and efficient purification method for alpha 2-antiplasmin is described that is based on the interaction between alpha 2-antiplasmin and a fragment from elastase-digested plasminogen constituting the three N-terminal triple-loop structures in the plasmin A-chain (LBSI). After a single-step adsorption of the alpha 2-antiplasmin from plasminogen-depleted plasma to LBSI-Sepharose and elution with 6-aminohexanoic acid, an 80-90% pure preparation with a yield of 50-60% is obtained. The major impurity is fibrinogen, which can easily be removed by gel filtration, and, as a result, a homogeneous fully active alpha 2-antiplasmin preparation is obtained that has the same properties as previously described for alpha 2-antiplasmin. Evidence is put forward that a form of alpha 2-antiplasmin with less affinity for the lysine-binding sites in plasminogen may exist, even in unfractionated plasma.
D002846:Chromatography, Affinity / Q000379:methods; D002850:Chromatography, Gel; D006801:Humans; D010196:Pancreatic Elastase; D010958:Plasminogen; D012685:Sepharose; D000979:alpha-2-Antiplasmin / Q000302:isolation & purification*
D000979:alpha-2-Antiplasmin; D010958:Plasminogen; D012685:Sepharose; D010196:Pancreatic Elastase