Purification of the plasmin receptor from human carcinoma cells and comparison to alpha-enolase.

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 M(r) 90 kDa [125I]-Pli to the surface of MCF7 cells with DSP results in the formation of a labelled complex of M(r) 145 kDa, suggesting a M(r) of 55-60 kDa for the receptor. Comparing Pli-R with alpha-enolase (a candidate for plasminogen receptor in U937 cells) we have found a high homology between both proteins, but not an identity.

• Authors: R Lopez-Alemany, P Correc, L Camoin, P Burtin
• Journal: Thrombosis research (Thromb Res) Vol. 75 Issue 4 Pg. 371-81 (Aug 15 1994) ISSN: 0049-3848 [Print] United States
• PMID: 7997975 (Publication Type: Comparative Study, Journal Article)

Chemical References

• Amino Acids
• Cross-Linking Reagents
• Receptors, Peptide
• plasmin receptor
• Phosphopyruvate Hydratase

Topics

• Amino Acid Sequence
• Amino Acids (analysis)
• Breast Neoplasms (blood, enzymology)
• Cross-Linking Reagents
• Humans
• Molecular Sequence Data
• Phosphopyruvate Hydratase (analysis)
• Receptors, Peptide (isolation & purification)
• Sequence Homology, Amino Acid
• Tumor Cells, Cultured