The　interaction　between　tamibarotene　and　bovine　serum　albumin　(BSA)　was　studied　using　fluorescence　quenching　technique　and　ultraviolet-visible　spectrophotometry.　The　results　of　experiments　showed　that　tamibarotene　could　strongly　quench　the　intrinsic　fluorescence　of　BSA　by　a　dynamic　quenching　mechanism.　The　apparent　binding　constant,　number　of　binding　site　and　corresponding　thermodynamic　parameters　at　different　temperatures　were　calculated　respectively,　and　the　main　interaction　force　between　tamibarotene　and　BSA　was　proved　to　be　hydrophobic　force.　Synchronous　fluorescence　spectra　showed　that　tamibarotene　changed　the　molecular　conformation　of　BSA.　When　BSA　concentration　was　1.00　x　10(-6)　mol　L(-1),　the　quenched　fluorescence　Delta　F　had　a　good　linear　relationship　with　the　concentration　of　tamibarotene　in　the　range　1.00　x　10(-6)　to　12.00　x　10(-6)　mol　L(-1)　with　the　detection　limit　of　6.52　x　10(-7)　mol　L(-1).　Copyright　(C)　2010　John　Wiley　&　Sons,　Ltd.