Formation and properties of C1‐inhibitor polymers
FEBS LettersPublished 24 July 1995
P A Patston, J Hauert, Monique Michaud, M Schapira
Citations42
SJR quartileQ1
SJR score1.22
SNIP0.77
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TL;DR
α1‐Antichymotrypsin, α2‐antiplasmin, angiotensinogen and thyroxine binding globulin also polymerised on heating, indicating that this is a property of many serpins.
Abstract
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.
Keywords
MedicineBiochemistry, Genetics and Molecular Biology
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