Formation and properties of C1-inhibitor polymers.
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.
Patston
P A
PA
Department of Oral Medicine and Diagnostic Sciences, University of Illinois at Chicago 60612, USA.
Hauert
J
J
Michaud
M
M
Schapira
M
M
D000911:Antibodies, Monoclonal / Q000276:immunology; D015153:Blotting, Western; D003174:Complement C1 Inactivator Proteins / Q000737:chemistry* / Q000276:immunology; D000939:Epitopes / Q000276:immunology; D010449:Peptide Mapping; D011108:Polymers; D011487:Protein Conformation; D011489:Protein Denaturation; D014357:Trypsin / Q000737:chemistry
D000911:Antibodies, Monoclonal; D003174:Complement C1 Inactivator Proteins; D000939:Epitopes; D011108:Polymers; D014357:Trypsin