Formation and properties of C1-inhibitor polymers

FEBS Lett. 1995 Jul 24;368(3):401-4. doi: 10.1016/0014-5793(95)00694-5.


Heating of the serpin C1-inhibitor above 55 degrees C induced the formation of inactive polymers. Western blotting of non-denaturing gels showed that the polymers bound to the conformation specific monoclonal antibody 4C3, suggesting that a similar conformational change to that occurring in complexed or cleaved inhibitor had taken place. N-Terminal analysis of tryptic peptides which bound to 4C3 showed that the epitope resides within residues 288-444, a region which includes parts of beta-sheets A and C. alpha 1-Antichymotrypsin, alpha 2-antiplasmin, angiotensinogen and thyroxine binding globulin also polymerised on heating, indicating that this is a property of many serpins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antibodies, Monoclonal / immunology
  • Blotting, Western
  • Complement C1 Inactivator Proteins / chemistry*
  • Complement C1 Inactivator Proteins / immunology
  • Epitopes / immunology
  • Peptide Mapping
  • Polymers
  • Protein Conformation
  • Protein Denaturation
  • Trypsin / chemistry


  • Antibodies, Monoclonal
  • Complement C1 Inactivator Proteins
  • Epitopes
  • Polymers
  • Trypsin