A novel, simple, and sensitive colorimetric method to determine aromatic amino acid aminotransferase activity using the Salkowski reagent
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu hodnotící studie, časopisecké články, práce podpořená grantem
PubMed
22130693
PubMed Central
PMC3297745
DOI
10.1007/s12223-011-0089-y
Knihovny.cz E-zdroje
- MeSH
- bakteriální proteiny chemie metabolismus MeSH
- enzymatické testy metody MeSH
- indikátory a reagencie MeSH
- kinetika MeSH
- kolorimetrie metody MeSH
- Pseudomonas putida chemie enzymologie MeSH
- transaminasy chemie metabolismus MeSH
- tryptofan metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- hodnotící studie MeSH
- práce podpořená grantem MeSH
- Názvy látek
- aromatic amino acid aminotransferase MeSH Prohlížeč
- bakteriální proteiny MeSH
- indikátory a reagencie MeSH
- transaminasy MeSH
- tryptofan MeSH
This study describes the development of a new colorimetric assay to determine aromatic amino acid aminotransferase (ArAT) activity. The assay is based on the transamination of L-tryptophan in the presence of 2-oxoglutarate, which yields indole-3-pyruvate (IPyA). The amount of IPyA formed was quantified by reaction with the Salkowski reagent. Optimized assay conditions are presented for ArAT isozymes isolated from Pseudomonas putida. For comparative purposes, ArAT activity was also determined by high-performance liquid chromatography. ArAT activity staining in polyacrylamide gels with the Salkowski reagent is also presented.
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