Further studies with human plasminogen

Publisher Website
Google Scholar
Abstract
Plasminogen has been purified by column chromatography with diethylaminoethylcellulose. The most active fractions were eluted with buffers containing 0.025 M-lysine resulting in preparations up to 500 times more potent than plasminogen in plasma. By paper electrophoresis it was shown that the active material is a minor component of the most active protein fractions.