Proteolytic activity assay based on enhanced peroxidase effect of hydrolyzed cytochrome c
Jazyk angličtina Země Velká Británie, Anglie Médium print
Typ dokumentu časopisecké články
PubMed
8395922
Knihovny.cz E-zdroje
- MeSH
- chymotrypsin metabolismus MeSH
- cytochromy skupiny c metabolismus MeSH
- endopeptidasy metabolismus MeSH
- kinetika MeSH
- pankreas enzymologie MeSH
- peptidové fragmenty metabolismus MeSH
- peroxidasy metabolismus MeSH
- prasata MeSH
- skot MeSH
- substrátová specifita MeSH
- subtilisiny metabolismus MeSH
- trypsin metabolismus MeSH
- zvířata MeSH
- Check Tag
- skot MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- chymotrypsin MeSH
- cytochromy skupiny c MeSH
- endopeptidasy MeSH
- peptidové fragmenty MeSH
- peroxidasy MeSH
- subtilisiny MeSH
- trypsin MeSH
A method using cytochrome c as the substrate of proteinases trypsin, chymotrypsin and subtilisin based on peroxidase effect of the formed haem octapeptide, which is much higher than that of cytochrome c, is described. The octapeptide is degraded by excess hydrogen peroxide and the competition between oxidation of guaiacol catalyzed by the octapeptide and octapeptide degradation leads under experimental conditions to rapid production of a stable colour. Absorption at 476 nm is proportional to proteolytic activity. The method was standardized using the Anson test for proteolytic activity with haemoglobin as a substrate.
