Counter Staining Of Peroxidase

In this experiment, the naturally occurring peroxidase is extracted from homogenized turnip (Brassica rapa) pulp (Coleman 2016). Its role in the environment is to remove toxic hydrogen peroxide during metabolic processes where oxygen is used (Coleman 2016). The goal of this experiment is to evaluate the change of absorbency of turnip peroxidase within a metabolic reaction utilizing oxygen. Any change noted is indicative of the peroxidase removing hydrogen peroxide. Within this experiment, the extract will be prepared, the amount of enzyme will be standardized, and the effect of changing the optimal conditions will be observed. If the enzyme concentration is increased then the rate of the reaction decrease. If the pH of solutions used is increased

The preparation for the experiment started by gathering the solutions of enzyme Peroxidase, substrate hydrogen peroxide, the indicator guaiacol and distilled water. Two small spectrometer tubes and three large test tubes with numbered labels. In addition, one test tube rack, one pipet pump and a box of kimwipes were also gathered. Before the experiment, the spectrometer must be set up to use by flipping the power switch to on. Following, the machine was warmed up for 10 minutes and the filter lever was moved to the left. In addition, I set the wavelength to 500 nm with the wavelength control knob. Before the experiment, I had to create the blank solution by pipetting 0.1 ml of guaiacol, 1.0 ml of turnip extract and 8.9 ml water into tube #1. Following the creation of the blank, a control 2% solution was created.

The data in proves that our hypothesis was correct. When we increased the temperature to 35°C, the the enzyme activity increased because kinetic energy increased, increasing the collisions between the substrate and the enzyme, and thus creating a higher chance of reaction. When we increased the temperature to 45°C, the enzyme activity decreased as the enzyme became denatured,because the atoms in the enzyme had enough energy to overcome the hydrogen bonds between the R groups that give the enzyme its shape From our data, we could conclude that the optimal temperature of turnip peroxidase is around 35°C and around 45°C, it will start to denature.

Horseradish peroxidase Type 1 was used in this laboratory experiment, it was an enzyme that helped catalyze the oxidative coupling of vanillin to produce divanillin. The role of the enzyme is to increase the rate of the overall chemical reaction to reduce reaction time, therefore making the reaction process faster. The Horseradish peroxidase Type 1 achieved this by decreasing the activation energy required for a chemical to react, thus allowing the reaction to process through a lower activation energy, which increases the reaction rate and makes the reaction faster.

Cells are the building blocks of life. Life itself would not be possible without cells and the actions they carry out. Hundreds of biological and chemical reactions take place in the cell every second. Most of the reactions in a cell use enzymes to speed up the reaction. An enzyme is a protein catalyst used by living organisms to increase the rate of biological reactions (Freeman et. al. 2016, p90). A catalyst brings substrates together in a precise orientation that makes reactions more likely. Enzymes have an “active site,” which is where the reactants bind to the enzyme. The active site is where catalysis occurs. The reactants of the enzyme are called the substrates. Enzymes are extremely effective at catalyzing reactions because

The purpose of this experiment is to learn the effects of a certain enzyme (Peroxidase) concentration, to figure out the temperature and pH effects on Peroxidase activity and the effect of an inhibitor. The procedure includes using pH5, H202, Enzyme Extract, and Guaiacol and calibrating a spectrophotometer to determine the effect of enzyme concentration. As the experiment continues, the same reagents are used with the spectrophotometer to determine the temperature and pH effects on Peroxidase activity. Lastly, to determine the effect of an inhibitor on Peroxidase, an inhibitor is added to the extract. It was found that an increase in enzyme concentration also caused an increase in the reaction rate. The reaction rate of peroxidase increases at 40oC. Peroxidase performed the best under pH5 and declined as it became more basic. The inhibitor (Hydroxy-lamine) caused a decline in the reaction rate. The significance of this experiment is to find the optimal living conditions for Peroxidase. This enzyme is vital because it gets rid of hydrogen peroxide, which is toxic to living environments.

One of the best-studied peroxidases is horseradish peroxidase (HRP), which has a heme-iron co-factor. In most heme-peroxidases the iron atom in the active center undergoes a reversible change of its oxidation state. The reaction proceeds in three distinct steps. In first step, the resting state high-spin Fe(III) is present, which is oxidized by hydrogen peroxide to form an unstable intermediate called compound I (Co-I) with Fe(IV), releasing water in the process. Compound I is not a classical enzyme–substrate complex, but rather a reactive intermediate with a higher formal oxidation state (­5 compared with ­3 for the resting enzyme). Thus, compound I is capable of oxidizing a range of reducing substrates. This reactive intermediate oxidizes

After electrophoresis was finished, my boss removed the gel casting tray from the running chamber. Then, she carefully transferred the gel to a DNA staining tray. My lab assistants and I were going to stain it so it would be easier to see the

In the meanwhile, in the cytoplasm, the hemagglutinin and neuraminidase have undergone glycosylation, polymerization, and acylation. The hemagglutinin, neuraminidase, and the matrix protein two (M2) all travel together to the plasma membrane. There the proteins meet with the other matrix protein (M1), and begin the

For this lab report, there's some unnecessary citation and commas almost in every section of the lab. For example, in the abstract section, there's an unnecessary in-text citation. Moreover, according to the lab manual, the abstract should include a little bit of everything such as the hypothesis, results, and methods. Which this lab report fails to do so this could be improved. In addition, the introduction part of the lab report was good. However, there were mistakes which include unnecessary commas, and space. At the end of the section, there's an awkward sentence "with the use of knowledge and understanding of chemical reactions....", this could be improved with

The author of this article wanted to investigate if Galectin-3 is involved in the development of skin lesion with a patient with systemic lupus erythematosus or SLE. Patients with SLE, dermatomyositis, systemic scleroderma and healthy person were studied. Galectin-3 in these group of people were examined using ELISA and immunohistochemical staining. Results shows that galectin-3 serum level is low in epidermis in skin lesion from a patient with SLE, dermatomyositis and systemic scleroderma compared to healthy person. According to their study, serum galectin-3 is not likely to be involved in skin injury in a patient with SLE but can be a biomarker for measuring the activity of the SLE disease. It is mentioned in the journal that Galectin-3

The experiment has done in lab is catalase, hydrogen peroxide, pH temperature, and liver. The enzyme are biological catalysts. Catalysts lower the activation energy for reactions. The lower the activation energy for a reaction, the faster the rate. Thus enzymes speed up reactions by lowering activation energy. The the reaction did in catalyze is the reactants of the subtrates were the hydrogen peroxide, and the products are oxygen gas and water. Because this interaction requires close physical contact between the enzyme and the substrate, most enzymes are highly specific so they only able to interact with one substrate and therefore only able to catalyze one type of chemical reactions. Also, the source of the enzyme were the plant, animal,

Our study showed a statistically significant association between the expression of galectin-1 and the site of tumor that 51% of specimens which showed high expression of galectin-1 were located at the upper pole. This may be attributed to that the majority of our studied tumors were located at the upper renal pole.

Enzymes are macromolecules that act as a catalyst, and it’s a chemical agent that accelerates the reaction without being consumed by the feedback or the results (Campbell and Reece, 2005). After the adjustment by the enzymes, the chemical movement through the pathways of metabolism will become awfully crowded because many chemical reactions are taking a long time (Campbell and Reece, 2005). There are two kinds of reactions in nature. The first one is Catabolic reaction and the second one is Anabolic reaction. Catabolic reactions are large molecules that are broken up into smaller molecules (Ahmed, 2013). Anabolic reactions are small molecules that join to make larger molecules, like polymerization (Ahmed, 2013). If you

Hydrogen peroxide is a toxic byproduct of cellular functions. To maintain hydrogen peroxide levels the catalase enzyme deconstructs hydrogen peroxide and reconstructs the reactants into oxygen gas and water. The catalase enzyme is found inside cells of most plants and animals. Regulating the levels of hydrogen peroxide is crucial in homeostasis and analyzing it’s optimal conditions for performance is just as important. To understand the optimal environment for this enzyme, they are put into different environments based off protein activity (enzymes are proteins). Catalase samples will be put into different hydrogen peroxide environments based off pH and temperature. The more active the enzyme, the more oxygen and water it will produce. Enzyme activity can be seen through the release of oxygen in the hydrogen peroxide. Since oxygen cannot be accurately measured, the data will consist of the longevity of the reaction in different environments. If the pH is higher than 7, then the reaction rate will increase due to the ample amount of hydrogen ions in the hydrogen peroxide. However the pH level cannot be higher than 10 or else there will be too many hydrogen atoms in the peroxide for the enzyme to be able to deconstruct them. If the temperature is increased, then the reaction rate will increase due to the ample amount of energy and movement in the hydrogen peroxide and enzyme.