Proteolysis and deglycosylation of human C1 inhibitor. Effect on functional properties.
The effects of proteolysis and deglycosylation on C1 inhibitor (C1Inh) were tested with respect to both its ability to form complexes with C1s and its capacity to block C1 autoactivation. Limited proteolysis of C1Inh by Staphylococcus aureus V8 proteinase, proline-specific endopeptidase or elastase generated a major high-Mr (approximately 86,000) fragment. In contrast with the fragment produced by elastase, which was inactive, the fragments resulting from V8 proteinase and proline-specific endopeptidase treatment retained activity. Deglycosylation with N-glycanase or O-glycanase, or both, had no major effect on the functional activity of C1Inh.
Reboul
A
A
Laboratoire d'Immunochimie-CEN-G, INSERM U238, unité alliée CNRS, USTMG, Grenoble, France.
Prandini
M H
MH
Colomb
M G
MG
D003174:Complement C1 Inactivator Proteins / Q000378:metabolism*; D003173:Complement C1s / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases; D006026:Glycoside Hydrolases; D006801:Humans; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis
D003174:Complement C1 Inactivator Proteins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D006026:Glycoside Hydrolases; C020668:glycanase; D010450:Endopeptidases; D003173:Complement C1s