Fluorimetric detection of enzymatic activity associated with the human tumor suppressor Fhit protein.
The human tumor suppressor Fhit protein exhibits diadenosine triphosphatase activity, hydrolyzing Ap(3)A to AMP and ADP. We report that Fhit protein efficiently cleaves the fluorogenic Ap(3)A analog diethenoadenosine triphosphate giving support to establish a simple fluorimetric assay for quantification of Fhit enzyme. Fluorimetric assays were initially tested to demonstrate that diethyl pyrocarbonate and suramin inhibit Fhit enzyme.
Departamento de Bioquímica y Biología Molecular, Universidad de La Laguna, 38206 La Laguna, Tenerife, Canary Islands, Spain.
A C
AC
Asensio
S
S
Oaknin
P
P
Rotllán
D017766:Acid Anhydride Hydrolases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D015226:Dinucleoside Phosphates / Q000737:chemistry; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D009363:Neoplasm Proteins / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry; D013050:Spectrometry, Fluorescence / Q000379:methods; D000099170:Bis(5'-adenosyl)triphosphatase
D017766:Acid Anhydride Hydrolases; D015226:Dinucleoside Phosphates; D009363:Neoplasm Proteins; D011506:Proteins; D011994:Recombinant Proteins; D000099170:Bis(5'-adenosyl)triphosphatase; C011440:diadenosine triphosphate