The interaction of fibroblast growth factor (FGF) with receptors on clonal-derived turkey embryonic and posthatch muscle cells was compared using saturation isotherms. 2. At least two binding sites, including a high affinity receptor and sites of low affinity, which are likely heparin sulfate proteoglycans, were observed on both embryonic myoblasts (EM) and myogenic satellite cells (SC). 3. The FGF binding affinities (Kds) were similar between SC and EM. Receptor Kds were also similar between SC derived from turkeys both selected and unselected for rapid, growth and skeletal muscle accretion rates.