Any feedback?
Literature summary extracted from
- Purified proenzyme C1r. Some characteristics of its activation and subsequent proteolytic cleavage (1980), Biochim. Biophys. Acta, 616, 116-129.
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.4.21.41 | after reduction and alkylation C1rbar undergoes proteolytic cleavage which lead to the successive removal of two fragments of 35000 Da and of 7000-10000 Da, leaving a divalent molecule of reduced size. The product C1rbar II retains the original antigenic properties of C1rbar and a functional active site, but loses the capacity to bind C1s | Homo sapiens |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.41 | Homo sapiens | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.21.41 | proenzyme C1r | Homo sapiens |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.21.41 | plasma | - |
Homo sapiens | - |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
