EC Number   |
Application |
Reference |
|---|
   3.4.24.33 | analysis |
analysis of isoaspartic acid by selective proteolysis with Asp-N and electron transfer dissociation mass spectrometry, overview. IsoAsp formation and repair is central to the survival and germination of plant seeds. Also once administered into patients and thus exposed to physiological conditions of pH 7 and 37 °C, protein pharmaceuticals, particularly those with long circulation time, may generate significant amount of isoAsp |
717087 |
| 3.4.24.33 | molecular biology |
many eukaryotic proteins are blocked at the alpha-amino group of their N-terminal with various modifications, thereby making it difficult to determine their N-terminal sequence by protein sequencer, development of a method for selectively isolating the blocked N-terminal peptide from the peptide mixture generated by endoproteinase AspN digestion of N-blocked protein by removal of all peptides other than the N-terminal one (non-N-terminal peptides) through their carbonyl group introduced by a chemical transamination reaction |
717082 |
| 3.4.24.33 | more |
AspN is shown to be an alternative protease for in-capillary digestion (during capillary electrophoresis), AspN behaves very similarly to trypsin |
-, 695579 |
