Synchronous luminescence: a simple technique for the analysis of hydrolysis activity of the fragile histidine triad protein

Human fragile histidine triad (FHIT) protein has dinucleoside 5',5'''-P-1,P -n-polyphosphates hydrolysis activity, with AMP being one of the reaction p roducts. Application of synchronous luminescence (SL) spectroscopy, in whic h both excitation and emission wavelengths are scanned simultaneously while a constant wavelength interval is maintained between them, was investigate d for detection of the enzymatic activity of the FHIT protein. Ability of S L to identify reaction components, AMP production and its increase as a res ult of increase in substrate concentration and inhibition of the hydrolysis activity by ZnCl2 are demonstrated.