The Interaction Mechanism between Human α2-Macroblobulin and Plasmin

P. Lambin, J. M. Fine, R. Audran, M. Steinbuch
1975 Thrombosis and Haemostasis Vth Congress   unpublished
When purified homogenous α2M is submitted to SDS polyacrylamide electrophoresis splitting in half molecules of MW of 380.000 is observed. If increasing amounts of plasmin are added to a given amount of α2M, a new component of MW 450,000 increases whereas as the MW 380,000 component decreases. This new component consists of one half molecule of α2M and one plasmin molecule. In the presence of reducing agents and SDS the half molecules of α2M are further cleaved showing that the molecule is
more » ... e molecule is composed of 4 chains having a MW of 180,000. If α2M/plasmin complexes are submitted to the same treatment, a major component MW of 95,000 appears proportionally to the amount of added plasmin. As already shown by Harpel this component is a split product to the proteolytic action of plasmin. Other components of major interest correspond to the heavy chain of plasmin MW 50,000 and a component of MW 120,000 which represents the association of the MW 95,000 fragment of α2M and the light chain of plasmin (25,000). This assumption is materialized by the use of Unlabeled plasmin. Both the 450,000 component and the 120,000 component are revaled by auto-radiography. Thus a stable, eventually covalent linkage between α2M and plasmin can be assumed.
doi:10.1055/s-0039-1689596 fatcat:i7dwoosd7fagfmsfkqhjglb27y