Application | Comment | Organism |
---|---|---|
analysis | nonspecific protease proteinase K can be used as an alternative to trypsin for cross-linking studies, digestion by proteinase K results in a family of related cross-linked peptides, all of which contained the same cross-linking sites, thus providing additional verification of the cross-linking results. Using proteinase K, the affinity-purifiable CID-cleavable and isotopically coded cross-linker cyanurbiotindipropionylsuccinimide and MALDI-MS cross-links are found for all of the possible cross-linking sites of native and oligomeric forms of prion protein substrates, overview. After digestion with proteinase K, the mass distribution of the crosslinked peptides is very suitable for MALDI-MS analysis | Parengyodontium album |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Parengyodontium album | P06873 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | substrate synthesis: a synthetic gene corresponding to the Syrian hamster prion protein sequence 90-232 with a 23-residue N-terminal fusion tag containing His6 and a thrombin cleavage site (MGSSHHHHHHSSGLVPRGSHMLE) is specifically synthesized and expressedas substrate for the enzyme | Parengyodontium album | ? | - |
? | |
prion protein + H2O | specific cleavage, that does not occur at cross-linker-modified residues | Parengyodontium album | ? | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Parengyodontium album |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | 8.5 | assay at | Parengyodontium album |
General Information | Comment | Organism |
---|---|---|
additional information | nonspecific protease proteinase K can be used as an alternative to trypsin for cross-linking studies, digestion by proteinase K results in a family of related cross-linked peptides, all of which contained the same cross-linking sites, thus providing additional verification of the cross-linking results. Using proteinase K, the affinity-purifiable CID-cleavable and isotopically coded cross-linker cyanurbiotindipropionylsuccinimide and MALDI-MS cross-links are found for all of the possible cross-linking sites of native and oligomeric forms of prion protein substrates, overview. After digestion with proteinase K, the mass distribution of the crosslinked peptides is very suitable for MALDI-MS analysis, detailed overview of cross-links in prion proteins | Parengyodontium album |