[Study on the interaction between vincristine and bovine serum albumin].

The interaction between vincristine (VCR) and bovine serum albumin (BSA) was investigated by UV-Vis absorption, fluorescence and circular dichroism (CD) spectra at 296, 303 and 310 K, respectively. With fluorescence quenching method, the binding constants Ka were determined to be 1.5 x 10(4) L x mol(-1), 9.

[Spectroscopy study on the interaction of colchicine and human serum albumin].

The binding reaction of colchicine with human serum albumin (HSA) was studied by UV-Vis absorption, fluorescence and circular dichroism spectrometry. The results indicated that colchicine led to the increase in UV absorption and the quenching of intrinsic fluorescence of HSA. As the temperature increased, the quenching constant Ksv decreased.