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. 1987 May 15;244(1):117–121. doi: 10.1042/bj2440117

Proteolysis and deglycosylation of human C1 inhibitor. Effect on functional properties.

A Reboul 1, M H Prandini 1, M G Colomb 1
PMCID: PMC1147961  PMID: 3311024

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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