Versatile Fluorescence Probes of Protein Kinase Activity

Journal of the American Chemical Society

Volumn 125, Issue 47, 2003, Pages 14248-14249

  Shults, Melissa D ^a   Imperiali, Barbara ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; MAGNESIUM; PROTEIN KINASE C;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; DNA PROBE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME LOCALIZATION; ENZYME PHOSPHORYLATION; ENZYME SUBSTRATE; FLUORESCENCE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; PROTEIN MOTIF; REPORTER GENE;

FLUORESCENT DYES; KINETICS; PEPTIDES; PHOSPHORYLATION; PROTEIN KINASES; SPECTROMETRY, FLUORESCENCE;

EID: 0344443386     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0380502     Document Type: Article

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23. 2+ concentrations other than 10 mM can be easily used following empirical determination of the percent fluorescence increase under the assay conditions.
24. 2+ dissociation constant can be used because the fraction of each peptide bound remains constant under these conditions. The absolute fluorescence signal of substrate and product peptides is linear with respect to concentration.