SPECTROSCOPIC STUDIES ON BINDING OF ANTHR AQUINONES AND FLAVONOIDS TOBOVINE SERUM-ALBUMIN

Stopped flow studies show that the binding equilibrium of emodin to bo vine serum albumin (BSA) is established within 100ms. The absorption m aximum of these compounds exhibit red shift upon binding and the absor bance enhanced. The fluorescence quenching associated with the binding of these compounds to BSA was used to measure binding constants, and the distance of Trp-212 to the first binding site were calculated, on the basis of the energy transfer between BSA and bound complexes. An a llosteric domain model of emodin-BSA complex was postulated.