Myosin is the primary motor protein in skeletal muscle, responsible for ATP hydrolysis that drives muscle contraction. In addition to force production, myosin consumes ATP during rest in futile cycles, a phenomenon associated with the Super Relaxed State (SRX), distinct from the disordered Relaxed State (DRX). The SRX is typically measured using the mantATP chasing technique, where the decay of a fluorescent ATP analogue is analyzed and fitted with a combination of exponential decay representing the biochemical states. While this method was initially applied to skinned muscle fibers, it has been adapted for simplersoluble myosin preparations, raising concerns about its reliability. Skinned fibers offer the advantage of preserving the native thick filament structure and myosin cooperativity, while mantATP's limited diffusion and non-specific binding pose challenges. In this study, we combine experimental data and in-silico modeling to dissect the contributions of different components in the mantATP chasing signal. We analyze both rabbit psoas skinned fibers and 'ghost' fibers, where myosin is extracted. Our analysis shows that the fast-decaying component of the signal reflects the effects of diffusion and non-specific binding, occurring on a timescale similar to that of DRX. In contrast, SRX nucleotide release is best described by an exponential decay, with the late timepoints primarily reflecting SRX characteristics. Our findings indicate that mantATP chasing reliably estimates SRX amplitude and time constant, as well as DRX time constant, although it may overestimate DRX amplitude in standard analyses