バナジウムおよび銅と血清アルブミンとの相互作用

抄録

The interactions of V⁴⁺ and Cu²⁺ with bovine serum albumin (BSA) were studied by means of circular dichroism (CD), UV, electron spin resonance (ESR) and fluorescence spectroscopy. The CD measurements showed that the interactions of BSA with V⁴⁺ were not influenced to both pH and temperature, and V⁴⁺ were changed to V⁵⁺ by the reaction with BSA at pH 7.4 and 37°C. The titration of V⁴⁺ effected to the Cu²⁺ second binding site (Cys 34) of BSA, but did not to the strongly Cu²⁺ binding site (N-terminal site) of BSA. These results suggest that V⁴⁺ has a high affinity to Cys 34 of BSA.