Abstract
We have characterized a receptor for plasmin (Pli-R) from a human tumor cell line, MCF7MF. The Pli-R was purified from a MCF7 0.1% Triton X-100 solubilisate by affinity chromatography. A protein of 55–60 kDa was obtained, which bound plasminogen and plasmin specifically. Chemical cross-linking of Mr 90 kDa [ 125I]-Pli to the surface of MCF7 cells with DSP results in the formation of a labelled complex of Mr 145 kDa, suggesting a Mr of 55–60 kDa for the receptor. Comparing Pli-R with α-enolase (a candidate for plasminogen receptor in U937 cells) we have found a high homology between both proteins, but not an identity.
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