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.
Research Article| May 15 1987
Proteolysis and deglycosylation of human C1 inhibitor. Effect on functional properties
M H Prandini;
Biochem J (1987) 244 (1): 117–121.
- Views Icon Views
- PDF LinkPDF
- Share Icon Share
- Cite Icon Cite
A Reboul, M H Prandini, M G Colomb; Proteolysis and deglycosylation of human C1 inhibitor. Effect on functional properties. Biochem J 15 May 1987; 244 (1): 117–121. doi: https://doi.org/10.1042/bj2440117
Download citation file: