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Literature summary for 3.4.21.41 extracted from
- Purified proenzyme C1r. Some characteristics of its activation and subsequent proteolytic cleavage (1980), Biochim. Biophys. Acta, 616, 116-129.
General Stability
| General Stability | Organism |
|---|---|
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| proenzyme C1r | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| plasma | - |
Homo sapiens | - |
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Release 2023.1 (January 2023)
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