Heparin and the progressive anti-thrombin activity of alpha 2-macroglobulin

Interactions between alpha 2-macroglobulin (alpha 2M) and thrombin have been studied by spectroscopic, isotopic and electrophoretic methods in presence or in absence of heparin. It is shown that thrombin binds to alpha 2M in a 1:1 ratio. Fluorescamin labelled heparin of Mr 7 000 interacts with thrombin to form a 2:1 molar complex. This complex does not bind to alpha 2M and is unable to achieve any proteolytic cleavage of this protein. In contrast the interaction of alpha 2M with chymotrypsin is not significantly affected by the mucopolysaccharide. Moreover, heparin is unable to react with alpha 2M bound thrombin.