both of the root imprints shown in figure 1 it appears that the highest

Both of the root imprints shown in figure 1 it

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both of the root imprints shown in figure 1, it appears that the highest concentration of peroxidase was contained within the epidermis and the cortex of the young dicot roots. Perhaps the radish plant requires the most peroxidase at the interface between the epidermis and external environment to efficiently and effectively neutralize harmful substances.Our nitrocellulose sheet containing the four peroxidase standards and root and leaf extracts (Figure 2) visualized more interesting results. Both the 100% experimental and 100% control root extract spots were similar in color density to peroxidase Standard 4. The 100% experimental leaf extract showed no indication of peroxidase presence. The 100% control leaf extract showed no peroxidase presence, yet did show presence of other proteins when stained with Ponceau S. These other proteins are stained red by Ponceau S and do appear to be present inthe 100% control leaf extract shown in Figure 2. Because no peroxidase was visualized in the leaf extracts, the leaf extracts were excluded from our hypothesis and we instead focused on our root extracts. One reason that peroxidase may not have been found in the leaf of both experimental and control radishes is that fluid uptake, and thus chemical uptake, mainly occurredat the root in the soil where their respective fluids were poured in to. Stress was minimized to theradishes above the soil and thus peroxidase may not have been needed.After electrophoresis ran for a duration of thirty-five minutes, the gel was placed on top of a table lamp and the relative positions of the standard proteins were visualized. Albumin migrated the farthest at 16 mm towards the anode. At pH 8.6 the protein caries a very negative charge and thus moves faster than the other two standard proteins. Cytochrome C migrated 14 mm towards the cathode. This was to be expected since at pH 8.6 the protein caries a net positivecharge. Finally, Hemoglobin migrated a distance of 6 mm toward the anode. At pH 8.6, this protein caries a negative charge.The peroxidase isoenzyme migrations on the gel were examined after incubation with peroxidase substrate solution. Two bands of the HRP-Basic isoenzyme were found, with a dark band migrating 2.5 mm to the cathode and the other lighter band migrating 2.5 mm to the anode. It was unexpected to find two bands for the HRP-Basic isoenzyme. A single basic peroxidase isoenzyme should have a net positive charge and thus migrate to the negative electrode. This anomaly could be caused by some forms of the protein in the solution having a net negative charge. Despite this, our research team concludes that the majority of the HRP-basic isoenzyme are net positively charged. As expected, two bands of the HRP-Mixture were found, both movingequidistant to the cathode and anode respectively at 2.5 mm each. The band that migrated to the
anode was found to be darker compared to the band that migrated to the cathode, indicating that the majority of peroxidase isoenzymes in the mixture are negatively charged. Both the

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