Guang Pu Xue Yu Guang Pu Fen Xi
August 2006
The interaction of alizarin yellow R(AYR) and bovine serum albumin (BSA) was investigated by fluorescence method in alkali buffer solution. It was shown that AYR had a powerful ability to quench the BSA fluorescence at excitation and emission wavelengths of lambda(ex) = 393 nm and lambda(em) = 641 nm in the medium solution of pH 11.00, and there were five binding sites of AYR to BSA; The combination reaction of AYR with BSA was a static quenching process, and from the effects of temperature on the fluorescence quenching rate of AYR-BSA and the Stern-Volmer quenching constant (K(SV)) and the Lineweaver-Burk quenching constant (K(LB)), the binding constant was calculated to be K = 1.
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