The phenomenon that charged particles migrate to electrodes with opposite polarities in an electric field is called electrophoresis. All kinds of protein in serum have their specific isoelectric points, but most of them are below PH7.0. If the serum is placed in a buffer with PH8.6, almost all protein will be negatively charged, and then it will move to the positive pole of your electric field. Due to the different charge amount, molecular size and shape of various proteins in the same PH environment, serum proteins can be divided into five regions, namely, a (albumin), α 1, 2, β and γ globulin from positive electrode to negative electrode. After electrophoresis, the cellulose acetate was placed in the dyeing solution. Protein is fixed and dyed, and then decolorized (washing away excess fuel). After the pulp is dyed, each area is cut separately, dissolved in alkaline solution, determined by colorimetry, and the percentage of each area is calculated.