A mini-gene encoding rat retinol-binding protein (RBP) and a cDNA encoding chicken purpurin were separately transfected into HeLa cells. In contrast to RBP, expressed purpurin did not bind to transthyretin (TTR). A purpurin/RBP hybrid protein was constructed by substituting the cDNA sequence encoding the N-terminal 29 amino acids of purpurin for the corresponding part of RBP. The expressed hybrid molecule bound to the TTR-Sepharose. These results demonstrate that purpurin does not bind to TTR, that a functional purpurin/RBP hybrid can be constructed, and that the N-terminal coil of RBP is not required for TTR binding.