Arginase Lab Report

Example of enzymes involved in biological processes are classified into; oxidoreductases, transferases, hydrolases, lyases, isomerase and ligases. Catalase an oxidoreductase and among the vital enzymes in the body, it catalyses the breakdown of hydrogen peroxide

The purpose of this experiment is to create a complete genomic library of Aliivibrio fisheri through the use of the lux operon. The examination of the lux operon gene occurs through the extraction of the DNA of Aliivibrio fischeri and digest a large piece of DNA to smaller random pieces. The fragment of DNA will later be ligated together in plasmid. Plasmid acts as vectors to transport DNA from one organism to another. The DNA will then run through a UV-visible spectrophotometer to test the absorbance of the extracted DNA.

Crystal violet was then added for 60 seconds before being washed off with water. The mordant, Gram’s Iodine, was added for another 60 seconds before getting washed off with water. The heat fixed smear was then washed with 95% alcohol until the wash ran clear, leading to the final step of adding Safranin for 45 seconds before being rinsed with water. The slide was finally blot dyed with bibulous paper before it was placed under a microscope to observe the color and shape of the bacterium. 2.2 Litmus Milk Reaction

Introduction: Enzymes are needed for survival in any living system and they control cellular reactions. Enzymes speed up chemical reactions by lowering the energy needed for molecules to begin reacting with each other. They do this by forming an enzyme-substrate complex that reduces energy that is required for a specific reaction to occur. Enzymes determine their functions by their shape and structure. Enzymes are made of amino acids, it 's made of anywhere from a hundred to a million amino acids, each they are bonded to other chemical bonds.

The products are released from the enzyme surface to regenerate the enzyme for another reaction cycle. The active site has a unique geometric shape that is complementary to the shape of a substrate molecule, similar to the fit of puzzle pieces.

The constants were the temperature, the amount of inhibitor, and pH. The equipment used includes a LabQuest Spectro Vis Plus, cuvettes, and 3 droppers containing various microliters. The experiment began by calibrating the LabQuest spectrophotometer at 500nm every 20 seconds for 120 seconds; this was to get the results on the absorbency amounts. Following that, cuvettes were filled each with 250 µl of peroxidase, 1000 µl of buffer (sodium phosphate), and 250 µl of indicator guaiacol. In each trial, there were 3 different amount of hydrogen peroxide: 250 µl, 500 µl, and 1000 µl. Before placing the hydrogen peroxide into the cuvettes, was important to have the cuvette in the spectrophotometer, ready to hit the 'record data' button as the reaction happened to quickly.

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

Many metabolic reactions, including protein synthesis, take place in the

From my findings we notice that the R2 value is 0.886 (shown in Figure 1) which indicates that there is a strong correlation between concentration of salivary amylase and how much light is absorbed. This suggest that due to the large amount of salivary

The Another medium used was MAC, it is used to isolate and differentiate gram-negative organisms and it is a pink, dusty rose color. Lastly, the Citrate Slant is a green color and it was used as a differential test to examine enzymes. The media were inoculated at 37°C for 48 hours, then it was observed to determine the

Enzymes speed up chemical reactions enabling more products to be formed within a shorter span of time. Enzymes are fragile and easily disrupted by heat or other mild treatment. Studying the effect of temperature and substrate concentration on enzyme concentration allows better understanding of optimum conditions which enzymes can function. An example of an enzyme catalyzed reaction is enzymatic hydrolysis of an artificial substrate, o-Nitrophenylgalactoside (ONPG) used in place of lactose. Upon hydrolysis by B-galactosidase, a yellow colored compound o-Nitrophenol (ONP) is formed.

Introduction: Enzymes are biological catalysts that increase the rate of a reaction without being chemically changed. Enzymes are globular proteins that contain an active site. A specific substrate binds to the active site of the enzyme chemically and structurally (4). Enzymes also increase the rate of a reaction by decreasing the activation energy for that reaction which is the minimum energy required for the reaction to take place (3). Multiple factors affect the activity of an enzyme (1).

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.

With the presence of NAD+, malate will then be transported into cytosol and will be converted back into oxaloacetate. The conversion will then reduces NAD+ into NADH and H+. The conversion from oxaloacetate into malate serve to move NAD+ from mitochondria into cytosol which is important in gluconeogenesis to proceed. In conclusion of this reaction, pyruvate carboxylase enzyme catalyzes the conversion of pyruvate into oxaloacetate in TCA cycle. But oxaloacetate needed to be converted into malate first before it can exit the mitochondria.

Ornthine is then carried back in the mitochondrial matrix and the cycle is complete. There are two nitrogens in urea. One nitrogen came from the ammonia produced in the mitochondrial matrix captured in the form of carbamoyl phosphate. The second nitrogen came from the α−amino group of the aspartate substrate in the reaction involving argininosuccinate synthetase. The carbon of the bicarbonate was the sole carbon of urea.