The characterization of the interaction between a ligand and its receptor is crucial for a broad variety of applications in academia as well as in the pharmaceutical industry. Although various sophisticated high-throughput technologies have been established to investigate the binding of ligands to their receptors, classical filtration-based receptor binding assays still have some advantages when smaller number of samples need to be tested. Here we describe a technically easy, cheap, and reliable receptor binding assay that was successfully applied to determine the binding constant of the NO-independent activator of soluble guanylate cyclase, cinaciguat, and the impact of other small molecules on its interaction with the enzyme.