Study On The Interaction Of Cu(Ⅱ),Sb(Ⅲ),Pb(Ⅱ) With Serum Albumin And Lysoeyme By The Single-weep Polarography And Its Application

Protein research is very important in life sciences. Proteins participate in every reaction and activity of organism. They are close and essential to the translation of hereditary code, the transmission of information and the replication of DNA. Quantitative analysis is the foundation of studying proteins. Simultaneously, that plays an important role in the assay of medicine, food and clinic. So, establishing a quick ,sirnple, sensitive to determine proteins is very valuable in application. Electrochemistry method has the advantage of quickness, convenience, sensitivity, and not being interfered by the color of the solution. Therefore, the Voltammetic behaviors and application of proteins were studied by polarography in this paper. The main contents included how Cu( II ),Sb(Ill), Pb( II) reacted with proteins and how a polarographic adsorption wave was yielded and its application in determines proteins. The results were as follows: 1. Investigation on the Polarogarphic anodic wave of protein-Cu complex and its application: In 0.05 molIL H2S04 solution, the complexes of Cu-proteins (such as BSA, HSA and Lyso.) gave a sensitive polargraphic anodic adsorption wave with the potential ?.45 V(vs. SCE) by single-sweep polarography. The peak current of the 1st differential wave was linearly proportional to the concentration of BSA and HSA in the range of 1.5x10~-9.0x10 mol/L .The correlative coefficient was 0.9991,0.9992 and the detect limit was i.5x109 mol/L respectively. There was a linear relationship between the current and Lyso's concentration in the range of 7.0x10~~3.0xl0~ moJIL, too. The correlative coefficient was 0.9994. The detect limit was 1 4x I 0~ molIL. The designed method is successfully applied to determine HSA in its sample. The study showed that the peak originated from Cu-protein (Cu: protein= 1:1) were adsorbed and oxided in the electrode 2. Investigation on the Polarogarphic wave of protein in NaOH solution in present of Sb(Ill)and its application: Proteins (BSA, HSA, Lyso ect.) reacted with Sb(llI) slowly in 0.08 molIL NaOH solution, but the reaction was quicked in boiling water. The product yielded a polarographic adsorption wave with -0.74 V(vs. SCE) of the potential. There was a linear relationship between the peak current and the concentration of proteins in the range of BSA(HSA): 3.0x10-4.5x10 molIL; Lyso :1.4x10 -2.1x1(Y mollL. The correlative coefficient was : BSA(HSA) 0.9996, Lyso 0.9992. The dect limit was 7.5x1010 molIL(BSA,HAS), 3.5x1(Y9 molJL(Lyso). The method is applied in assaying HSA in samples and the result is the same to that of Classical Bradford method. The peak was proved to be Sb(Ill)- complexes adsorption reduced wave. 3. Investigation on the Polarogarphic wave of Pb( II )enatured protein and its application: In 0.5 molILNaOH solution, protein(BSA,HAS,Lyso) and Pb(ll) set in boiling water for 5 minutes had reaction. The production formed a polarogapraphic adsorption wave with the potential -0.63 V(vs. SCE), and added (C4H9)4.N1 (0.02% w.t.), eliminated the influence of the following wave of the dissociate Pb( II), and improved its sensitivity. The 1st differential peak current was linearly in proportion to the concentration in the range of 7.5x1&-3.0x1 moIJL (BSA, HSA) 1.4x1041.3x1Ci?moIIL (Lyso). The correlative coefficient was 0.9995 (BSA), 0.9990(HSA), 0.9997 (Lyso). The detect limit was 3.OxlO10molfL (BSA and HSA), 7.0x1(Y mol/L (Lyso) respectively. The determination of HSA in sample is satisfactorily achieved by using...