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Literature summary for 3.1.21.1 extracted from
- The N-terminal fragment of gelsolin inhibits the interaction of DNase I with isolated actin, but not with the cofilin-actin complex (2005), Proteomics, 5, 3131-3136.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 2 chromatography steps to homogeneity | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| cell culture | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| double-stranded DNA + H2O | the N-terminal fragment of gelsolin disrupts the actin-DNase I interaction in vitro. Colfilin stabilizes the actin-DNase I complex preventing release of DNaseI from actin by gelosin in vitro | Homo sapiens | 5'-phosphooligonucleotides + ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DNase I | - |
Homo sapiens |
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Release 2023.1 (January 2023)
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