The line towards their oppositely charged electrode. There were

The results, as seen in Figure 1, show the standard serum samples contained proteins and the test sample only contained y-globulin. Y-globulin was attracted towards the cathode, meaning that they were positively changed. Albumin was the most abundant, the fastest moving band, the heaviest shown in the lane and was negatively charged as it migrated towards the cathode. Alpha and beta globulins show they were attracted to the anode, due to their positive charge. The molecular weights for proteins; albumin weighting the lowest at 66.5 kDa and gamma weighting the highest at 1193kDa. The gel shows standard serum containing proteins worked as the bands are defined.

The test sample contained immunoglobulins, which moved the furthest away towards the cathode. Y-globulin is an immunoglobulin and is part of the humoral immunity. Gamma globulin was darker in the test sample indicating an increase of y-globulin. The proteins reacted opposingly as they migrated from the injection line towards their oppositely charged electrode. There were no abnormal proteins detected as results showed separation of proteins.  If abnormal y-globulin (IgM) was found, it would suggest the patient has monoclonal gammopathy. An increase in protein can identify dehydration, diarrhea whereas a decrease can detect liver disease etc. In this case, y-globulin was detected; the patient could have an immune deficiency. The bands in lane 1 show multiple proteins as there are many bands. Lane 4 has the least number of bands showing a small number of proteins.

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Limitations are that the gel does not specify the amount of protein in the blood. The gel doesn’t show specific proteins as there are diverse types of gamma proteins. Another purifying method to be used to identify the exact protein. As gel is delicate it increases the chances of damage to the gel. The experiment could have been repeated for more accurate results. The gel was damaged whilst blotting and was replaced so the results are not affected.

The advantages of Serum protein electrophoresis are simple, quick and non- expensive. The gels are commercially produced. Many samples can be made using the same gel. The disadvantages of serum protein electrophoresis are low resolution and proteins not being specific.

In the future, other methods such as urine electrophoresis can be used in addition to detecting more specific details.