ipl-logo

Arginase Lab Report

1437 Words6 Pages

INTRODUCTION: Arginase is an enzyme- enzymes are biological catalyst which drives a reaction at the speed of life. Arginase is a hydrolase, hydrolases catalyze hydrolysis reactions, this is determined via the E.C number (Nelson and Cox 2008). Arginase has the EC number is 3.5.3.1 (Schomburg 2015). The enzyme ‘commission number’ is the arithmetical classification that is used for enzymes which indicates the chemical reaction they catalyze. EC 3 are hydrolases, which forms two products from the substrate via hydrolysis. (Bach, et al. 1961) This is seen in the equation: L- Arginine + H2OL-Ornithine + Urea (Nelson and Cox 2008). The urea cycle is the procedure where ammonia is transformed into to urea. Throughout the urea cycle, the amino acid, arginine, is changes into ornithine- this is another amino acid when hydrated, that is when water was added. During this reaction, urea is the product formed (Nelson and Cox 2008). Figure 1 shows the urea cycle, occurs specifically in the mitochondria and cytosol in the liver. (Nelson and M.Cox 2008). Urea is made in the liver by means of enzymes in the urea cycle. The enzymes that is associated with the urea cycle are; carbamoyl phosphate synthesase, …show more content…

The reaction that occurs can be investigated via the adding of the liver extract which contains the arginase to urea concentrations and distilled water. The amount of urea formed is determined via spectrophotometric analysis α-INPP. The urea produced was known via the color reaction with the α-INPP, it is the reagent used for the colorimetric determination of urea. (Barry J, et al. 1984). The red color formed when the α-INPP is reacted with the urea, is sensitive to light thus it is photo labile. The absorbance level @ 520 nm obtained from the spectrometer indicates the amount of urea obtained via measuring the absorbance of the light through the supernatant coloration, which was provided by the

Show More
Related
1410 Words | 6 Pages

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

Read More
251 Words | 2 Pages

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.

Read More
1090 Words | 5 Pages

Each amino acid is made up of an amino group, a carboxyl group and a side chain (Reece, J. B., Urry, L. (2016). Campbell biology. Boston Pearson). Enzymes work by lowering the activation energy of the reaction making the reaction produce faster. Enzymes begin to catalyze chemical reactions with the binding of the substrate to the active site on the enzyme.

Read More
855 Words | 4 Pages

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

Read More
795 Words | 4 Pages

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.

Read More
494 Words | 2 Pages

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

Read More
429 Words | 2 Pages

Practical Activity Outline: Predicting the Effect of pH on the Activity of Amylase Arlecia Johnson Enzyme to use: Amylase is the easiest enzyme to find, it is in your saliva! Source: Saliva Animal: Human being The substrate: Starch, because amylases action starch and starch is also very easy to find in carbohydrate foods. Method and type of treatment A. Position a drop of solutions of iodine in test tubes (each with one drop) and place them in a row, in a test-tube rack.

Read More
750 Words | 3 Pages

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).

Read More
491 Words | 2 Pages

Enzymes are needed for both plant and animal life. There would be no life without enzymes (Wolfenden & Snider, 2001). The rate of an enzyme reaction is

Read More
971 Words | 4 Pages

Enzymes consist of an active site, this active site is unique to the substrate which it binds to. The active site is a tertiary structure which defines what substrate can bind to the active site. The active site is therefore highly specific. The structure and function of enzymes are compared to the lock and key hypothesis, where the lock is the enzyme and the key being the substrate. Another theory which has been presented is the induced fit hypothesis, where the tertiary structure in the active site changes slightly when bonded to the substrate to strengthen the bond between the active site and the substrate.

Read More
1114 Words | 5 Pages

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

Read More
1046 Words | 5 Pages

Along with being found in plants, they are also present in liver cells, kidney cells, leukocytes and erythrocytes. For the concentration of enzyme experiment, the hypothesis was if the concentration of an enzyme increases, then the enzyme activity will increase as well. The hypothesis was proven to be true, because there are more enzymes to react with substrates. For the enzyme—factors affecting, the hypothesis concluded was if the temperature increases, than the enzyme activity will increase. This however was proven wrong, because enzymes become unstable at higher temperatures.

Read More
1026 Words | 5 Pages

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.

Read More
1344 Words | 6 Pages

The fumarate that is produced in the arginosuccinate lyase reaction is an intermediate of the TCA cycle. There are many ways by which this fumarate produced in the cytosol is transported across the inner mitochondrial membrane into the mitochondrial matrix INHERITED DEFICIENCIES IN THE UREA CYCLE: There are many inherited diseases of the urea cycle that occur by mutations in the genes that encode any enzyme necessary for this cycle The most common among these is an inherited deficiency of ornithine transcarbamylase, which is an enzyme required for the conversion of ornithine to citrulline. It results in increased levels of ammonia which may be so high as to be

Read More
1057 Words | 5 Pages

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

Read More

More about Arginase Lab Report

Open Document