Screening tools for the development of new cancer therapies are in high demand worldwide and often require the determination of enzyme kinetics. The high sensitivity of lanthanide luminescence, particularly of time-resolved luminescence has revealed to be an ideal candidate for this purpose. There are several ways of conducting this analysis by the use of fluorogenic enzyme substrates, substrates bearing donor/acceptor groups allowing fluorescence resonance energy transfer (FRET) and immunoassays. For example, guanine nucleotide binding proteins consist of several subunits, one of which comprises those of the Ras subfamily. Ras GTPases act as binary switches by converting guadenosine triphosphate (GTP) into guadenosine diphosphate (GDP). Luminescence of the Tb(III) complex with norfloxacin is sensitive to determine the concentration of phosphate released by the GTP to GDP transformation.