The interaction of Zincon(ZCN)-Cu(Ⅱ) metal complexe with bovine serum albumin (BSA) was investigated by UV-Vis spectrophotometric method in acidic buffer solution (pH=4.25). ZCN-Cu(Ⅱ)-BSA was a blueness color coordination compound, with maximum absorption at 605 nm with 10 nm, 60 nm and 140 nm of red shift compared to the ZCN-Cu(Ⅱ) complex, ZCN-BSA complex and ZCN. According to molar ratio method and dual wavelength method, the apparent molar absorptivity of ε was equal to 4.82×105 L·mol-1·cm-1. Conditional constants were defined as ZCN∶Cu(Ⅱ)∶BSA=10∶5∶2. Condition combination constant of ZCN-Cu(Ⅱ) and BSA K was 8.82×104. A combined mechanism was suggested between BSA and ZCN-Cu(Ⅱ) by electrostatic force (Primary action force) and distant water force. Position of Impact might be arginine, proline, histidine, tyrosine and cystine. Contemporary formation of electron transfer complexes is an important cause in forming ZCN-Cu(Ⅱ)-BSA complexes.
The binding reaction of cytidine 5′-phosphate(5′-CMP) with Alizarin Red S(ARS) was studied in the buffer solution(pH=4.56) as functions of temperature, time, ionic strength and interference of inorganic substance, biological substance and surfactant by UV-Vis spectrophotometry. It was found that the bathochromic shift of the maximum absorption peak of the complex was 90 nm. The apparemt molar absorptivity wasε=3.80 ×10^3L/(mol·cm), the binding number was n=13, and the linear range of reaction was 0～14mg/L.
