Any feedback?
Literature summary for 3.4.21.38 extracted from
- The low pH stability of human coagulation factor XII (Hageman factor) is due to reversible conformational transitions (1994), Thromb. Res., 75, 259-268.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | factor XIIa undergoes large changes in secondary structures when exposed to low pH in the presence of dextran sulfate 500. The reaction of factor XII with dextran sulfate 500 at pH 5.3 results in loss of alpha-helical structure while at pH 8.3, in its formation. At pH 5.3 autoactivation is inhibitited. This may indicate that alpha-helical structure in factor XII plays an important role in the autoactivation mechanism | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| 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
