Ontology highlight
ABSTRACT:
SUBMITTER: Luzi NM
PROVIDER: S-EPMC5889107 | biostudies-literature | 2017 Sep
REPOSITORIES: biostudies-literature
Luzi Nicole M NM Lyons Charles E CE Peterson Darrell L DL Ellis Keith C KC
Analytical biochemistry 20170605
Here we describe a convenient, inexpensive, and non-hazardous method for the measurement of the kinase activity of the catalytic subunit of cAMP-dependent protein kinase (PKACα). The assay is based on the separation of a substrate peptide labeled with a strong chromophore from the phosphorylated product peptide by high-performance liquid chromatograph (HPLC) and quantification of the product ratiometrically at a wavelength in the visual spectrum (Vis). The utility and reliability of the HPLC-Vis ...[more]