Abstract
Summary
Human α2-macroglobulin can be dissociated by dialysis against 3 M urea into two 11S subunits which remain stable under physiologic conditions. These subunits retain kallikrein inhibitory capacity albeit at a reduced level when compared with the native protein. They furthermore protect bound kallikrein from further inhibition by native α2-macroglobulin. Bound kallikrein can not be dissociated from either the subunits or the native protein by Sephadex G-200 gel filtration.
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