| Abstract: | Spectropolarimetric studies of alpha 2-antiplasmin in the far ultraviolet region indicates a content of 16% alpha-helix, 18% beta-structure and 66% random coil. Two of its three disulphide bridges are reduced under non-denaturing conditions without major changes in conformation of functionality. Cleavage of the third disulphide bridge requires denaturing agents and is accompanied by complete loss of activity. The interaction of alpha 2-antiplasmin with plasminogen or fragments derived from plasminogen by elastase digestion has been studied by circular dichroism analysis in the near ultravoilet region. The results indicate that the fragment of plasminogen constituting the three NH2-terminal triple-loop structures contains at least two lysine-binding sites: one with high affinity and one with low affinity. One of these sites, probably the high-affinity site, is involved in the interaction with alpha 2-antiplasmin. This site seems also to be exposed in the intact plasminogen molecule. The formation of the stable complex between plasmin (EC 3.4.21.7) and alpha 2-antiplasmin is also accompanied by conformational changes. |
