The Impact of Malonate on SDH Activity Hypothesis: We hypothesize that the reagent malonate will inhibit, or decrease SDH activity. Justification: Succinic dehydrogenase is an enzyme that is bound to the inner membrane of the mitochondria and takes part in the Krebs Cycle as well as the Electron Transport Chain. Most importantly, SDH is a major component in the Krebs Cycle, and catalyzes the oxidation of its succinate ions to fumarate ions, changing its chemical composition from C4H4O4 to C4H2O4, by removing hydrogen ions. ("5. Enzyme Inhibitors,” 2013). The introduction of malonate can decrease succinic dehydrogenase activity by acting as an inhibitor. This is because the malonate will block the substrate succinate from reaching the enzyme. The result of this interaction yields no product and succinic dehydrogenase activity decreases. This type of inhibition can be called competitive because only one of the substrates can bind to the enzyme. In a study conducted at the McArdle Memorial Laboratory in Wisconsin, researchers found that the malonate did not damage the enzyme because the enzyme-substrate complex was similar to that of succinate. Malonate has the chemical composition C3H2O4-2 compared to the C4H4O4 composition of succinic dehydrogenase (Potter and Dubois, 1943). …show more content…
In a study from 2013 diazoxide and malonate were both used to test succinic dehydrogenase activity in the mitochondria of wild mice. Both diazoxide and malonate inhibited succinic dehydrogenase activity in the mitochondria of wild-type mice. Tests showed that malonate and diazoxide both decreased succinic dehydrogenase activity, however malonate decreased succinic dehydrogenase activity at a lower rate than diazoxide. Malonate absorbance showed to decrease approximately ten percent, whereas diazoxide absorbance decreased approximately fifty percent. (Anastacio, et. al.
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Based on the observation that the tubes containing PTA and citric acid were the only tubes that showed no color change, it was assumed that the ion of copper that the two the chelating agents bonded was necessary for the reaction. Otherwise, if it was not necessary, color change, from clear to brown, would have occurred signaling that the enzyme, catecholase, did catalyze the conversion of catechol to benzoquinone. The purpose of this experiment was to determine which ion(s) bonded by the three chelating agents was the necessary cofactor(s) to the enzyme catecholase. Since the presence of benzoquinone causes the appearance of a brown color, we used this factor to determine whether or not the reaction occurred-by which catecholase was to catalyze.
ATP content and mitochondrial respiration will be measured ex vivo in rats selected from Experiment 2A at each time point (0-3 hours, 2 and 7 days) to determine the effects of melatonin on mitochondrial energetics and ROS production. Data generated will allow a comparison to be done of ex vivo ATP content and mitochondrial respiration rates in lesion versus non-lesion with in vivo measures of ATP status obtained using MRI in the same rat. Comparison will be made between saline and melatonin treated rats. Experiment 1C: To determine the impact of mono therapy (Melatonin) following TBI on apoptotic markers. Fluro Jade B and Nissl staining will be measured ex vivo in rats selected from Experiment 1A at each time point (0-3 hours, 2 and 7 days) to determine the effects of melatonin on apoptosis.
This catalyst is necessary for an aerobic organism to survive in aerobic conditions. After the experiment it was observed that my Gram positive organism did in fact bubble and utilize catalase. The third test conducted was on the MSA agar. This test was conducted for the purpose of selective and differential whether or not my organism can tolerate high salt concentrations. It is based on the mannitol fermentation.
The objective of this experiment was to perform a dehydration of 2-methylcyclohexanol. The result would be a mixture of 1-methylcyclohexene and 3-methylcyclohexene. There can also be a third product, methylenecyclohexane, though this would be identified using gas chromatography. An acid-catalyzed dehydration of 2-methylcyclohexanol occurs via an E1 mechanism; acids will react with 2-methylcyclohexanol to eliminate the alcohol (OH group). This causes the formation of a carbocation and an alkene will form near the charge.
As with all proteins, the enzyme has a 3D shape that is effected by the enzymes environment in many ways. Temperature is one of the major factors in an enzymes environment, when it is in its most suited environment it will function at its full potential. Changing that environment
Abstract The purpose of this experiment is to test for mitochondrial activity by isolating different organelles using the differential centrifugation process. Studying mitochondria is extremely important because they control the death and life of the cell by regulating the apoptotic signals (Frezza et al 2007). Also they are responsible for the metabolic reactions (aerobic respiration) and the production of ATP (Frezza et al 2007). Three hypotheses were formed based on my knowledge.
Oxidative Phosphorylation is the metabolic pathway in which mitochondria use their structure, enzymes, and energy released by the oxidation of nutrients to create ATP. If cells become oxygen deficient, the condition known as hypoxia (no oxygen) occurs. This condition can be due to abnormally acidic blood or a lack of critical enzymes necessary for releasing oxygen from red blood cells, so when this oxidative cycle is oxygen deficient, it can’t produce the quantity nor quality of ATP necessary for normal cellular functioning. “Oxygen is alkaline forming in the blood, while carbon dioxide which is produced as a by-product of the oxidation process is acid forming.
Nevertheless, the effects caused by the breakage of bonds will eventually lead to a decrease in the rate of reaction. As seen in the data, the reaction rate increased from 0.088 to 0.101 throughout the interval of -5℃ to 20℃ then decreased to 0.037 throughout the interval 20℃ to 56℃. This can be explained by the fact that 20℃ is the optimal temperature, therefore the active site of the enzyme is complementary to the substrate, causing the rate of reaction to be
Alcohol metabolism in the liver will produce a large number of free radicals, excessive free radicals scavenging ability than the body, will react with the cell membrane, causing lipid peroxidation, resulting in damage to liver cells, liver cells and enzymes are released into the blood, related serum biochemical index increased. From the results of this experiment, compared with the blank group, the levels of ALT and AST in the liver of the model group were increased, and the difference was statistically significant (P<0.01), which showed that the alcoholic liver model was successful. The administration group could promote the increase of GSH-PX and SOD activity in the liver of mice, and inhibit the increase of MDA content in liver tissue, and then protect the protective effect of acute alcoholic liver injury in
Hepatic acetylation is the main path of the isoniazid metabolic pathway, with the action of N-acetyl transferase that produces acetylisoniazid. Acetyisoniazid is then hydrolyzed to isonicotinic acid that is conjugated with glycine, and acetylhydrazine, both are excreted in the urine. Acetylhydrazine will be then metabolized to diacetylhydrazine and the hepatic microsomal enzymes may convert it to a hydrazine, which is a reactive metabolite that is responsible for the isoniazid-induced hepatotoxicity. Acid labile hydrazones that are formed with a-ketoglutarate and pyruvate produced in the bladder because they don’t appear in the blood.
The competitive inhibitor that was added was lactose. We predicted this because competitive inhibitors block and bind to the active site so it will slow down the binding of the desired substrate. An alternative hypothesis that came up was that the reaction of substrate would stay consistent as if no inhibitor was added. The enzyme could reject the inhibitor if it does not fit in the active site, causing the substrate to bind as it normally would. Our results showed that with the addition of lactose, the reaction did slow down a considerably
Excessive salt concentration will affect the hydrogen bond in the active site of enzyme. The enzyme will be denatured that the substrates cannot bind the the active site . Errors: There may be some errors in this experiment , the amount of amylase in the saliva may not be enough to breakdown the starch. Therefore, there may be difference between the text result and expected result. Conclusion:
ABSTRACT: The purpose of the experiments for week 5 and week 6 support each other in the further understanding of enzyme reactions. During week 5, the effects of a substrate and enzyme concentration on enzyme reaction rate was observed. Week 6, the effects of temperature and inhibitor on a reaction rate were monitored. For testing the effects of concentrations, we needed to use the table that was used in week 3, Cells.