Therefore, each of the three samples (real one, imitation, and unknown) were placed in a mortar with 1,5 ml of sample preparation buffer, and then the mixtures were ground with the help of a pestle. Afterward, they were poured into a 15 ml centrifuge in order to pellet the solids. Then 15 Î¼l of each sample were loaded into the wells. The electrophoresis procedure lasted for about half an hour. The apparatus was run at 170 volts (Carpenter et al, 2007). Subsequently, the gel was covered with a destaining solution and this enabled us to see the banding patterns. Given that the charge is the same, the only factor that affects the migration of protein is the molecular weights. The smaller protein would travel faster than a larger one. Nevertheless, one should not forget that degradation of samples or overconcentration of polyacrylamide may change the speed of migration.
Theoretically, other determinants influence the mobility of a protein, namely, their charge on their native form but due to the use of buffer this effect is reduced to a minimum. It should be pointed out that the charge of the buffer is never equal to that of one of the proteins (Stanley, 183). Furthermore, if these samples were run on a gel with a higher percent of agarose, the whole process would be showered and it will also change the distance between the bands. The increased percentage of agarose is more suitable for other types of electrophoresis. These are the hypothetical limitations of gel electrophoresis, yet, it seems that all of these pitfalls were avoided in the course of the experiment. So, the findings that we have obtained can be considered valid.
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