Lab Report On Protein Purification

If feeding efficiency and reproduction have a direct correlation, and a population started with equal proportions of individuals with each of three feeding types, metal spoon, metal knife, and plastic fork, the frequency of the population with metal spoons as their feeding structure will increase in the next generation. While the frequency of metal knifes and plastic forks will decrease. Furthermore, since the organisms with the metal spoon feeding structure have a higher fitness level, this population will evolve by natural selection to a point where the metal spoon phenotype will be in abundant. While the organisms with metal knifes and plastic forks phenotypes will decrease in frequency due to the lack of reproduction. Eventually, if this population persist overtime, most of the organisms, if not all, will have the metal spoon phenotype, while very few, if not any, will have the metal knife or the plastic fork phenotype.

The enzyme lactate dehydrogenase (LDH) catalyzes the last step of anaerobic glycolysis that is important for the normal function of the body. Purification of LDH is essential to understand its structure and function. The purpose of this experiment was to extract and purify LDH enzyme from chicken muscle tissue using a variety of various. Analytical methods such as activity and protein assay were employed to determine the presence and purity of LDH. The cells were initially disrupted and proteins were solubilized. LDH was purified from the ammonium sulfate precipitated protein mixture by affinity chromatography and its activity was studied by

Understanding the activity of enzymes in different muscle types can aid greatly in obtaining more information about other processes such as metabolism of the tissues (Anderson et al., 2012). There are many different methods in order to achieve this information based in two different major categories but the most convenient method is one called continuous assay. This process includes the use of a spectrophotometer to continuously monitor the assay. This method allows for an easy way to calculate the initial rate of reaction as one can establish time points easily. In the lab performed the continuous method was used in order to determine the measurement of the activity enzyme succinate dehydrogenase (SDH). SDH is most commonly found in mitochondria. It is present in many different muscle tissues including the heart, red, and white tissue. In the following lab the enzyme was tested and measured in these three muscle types in the Oncorhynchus mykiss in order to determine which type contained the highest and the lowest activity. This enzyme is involved in multiple processes such as involved in both the Krebs cycle and the electron transport chain (ETC) (Smith, 2014). Its role in

Enzymes are catalysts that function to speed up reactions; for example, the enzyme sucrose speeds up the hydrolysis of sucrose, which breaks down into glucose and fructose. They speed up reactions but are not consumed by the reaction that is taking place. The most important of the enzyme is the shape as it determines which type of reaction the enzyme speeds up. Enzymes work by passing/lowering and energy barrier and in doing so; they need to bind to substrates via the active. Once they do, the reaction speeds up so much more quickly than it would without the enzyme. Coenzymes and cofactors aid the enzyme when it comes to binding with the substrate. They change the shape of the active site so the substrate can bind properly and perform its function.

One of the most significant reactions in Glycolysis is reaction one which involves the phosphorylation of glucose to form glucose-6-phosphate. Through the transfer of the hydrolysis of ATP, this supplies energy for the reaction and makes it essentially irreversible, having a negative free energy change, which allows for a spontaneous reaction in cells. Although the preparatory phase is energy consuming and uses up 2 ATP, the pay off phase synthesizes 4 molecules of ATP, with the transfer of 4e- via 2 hydride ions to 2 molecules of NAD+. Therefore, a net gain of 2 ATP is achieved through the glycolytic pathway alone. Following the glycolytic pathway, due to the absence of oxygen, as oxygen cannot be supplied fast enough to undergo aerobic respiration, the athlete will instead, undergo lactic acid fermentation. Lactic acid fermentation involves pyruvate that is formed from the glycolytic pathway to be reduced to lactate, with the aid of the enzyme, lactate dehydrogenase, while the coenzyme Nicotinamide Adenine Dinucleotide (NADH) is oxidised to NAD+. The product NAD+ then re-enters the glycolytic pathway in order to produce 2 ATP. This process of lactic acid fermentation produces 2 ATP for each cycle, and thus, rapidly supplies the body with a small amount of energy. However, with the buildup of lactic acid in the body, the athlete will eventually encounter the feeling of discomfort as this accumulation of lactate causes the body to

2. We measured 1 mL of turnip peroxidase (the enzyme) and 3 mL of neutral buffer (pH corresponding to the test tube number i.e. pH 5 in test tube 5) with a syringe and disposed it into tubes 3, 5, 6, 7, 8, and 10

The optimum pH level would be pH 7. This is because this is where the highest amount of enzyme activity is taking place.

Observation: no bugs were found except small, black, gnats were all close to the ground.

An association between enzyme production, gene copy number, and gene evolution was explored by conducting analysis of the salivary amylase enzyme, AMY1A gene copy number, and the ancestral starch consumption in Homo Sapiens (Tracey 2017, p.22). It was hypothesized that the relative amount of starch consumption was very high for my personal ancestral diet, thus my AMY1 diploid gene copy number in my genome and salivary amylase concentration would be significantly higher than the population mean. With a population of 28 subjects (n=28), individual saliva samples were collected and compared to a calibration curve to determine the approximate amylase concentration by analyzing absorbance values. Individual samples of buccal cheek cells were

Ps: the iodine was already really dark so it was very hard to see much difference between the control and the others.

Use a test tube holder to put the test tube into a container of boiling water for 5 minutes, or until the solution changes color.

In part II of the lab six small glass tubes were obtained in a test tube rack. Ten drops of distilled water were then added to test tube 1, five drops to tubes 2-4, and no drops in tubes 5 and 6. Five drops of 0.1M HCl were added to test tube 5 and five drops of 0.1M NaOH to test tube 6. Five drops of enzyme were then added to all tubes except tube 1. Tube 3 was then placed in the ice bucket and tube 4 was placed in the hot bucket at 80-900C for five minutes, the remaining tubes were left in the test tube rack. After the five minutes five drops of 1% starch was added to every tube and left to sit for ten minutes. After ten minutes five drops of DNSA were then added to all the tubes. All the tubes were then taken and placed in the

In UNIT 7 you learned about the basics structure as well as the basic functions of deoxyribonucleic acid. You learned that deoxyribonucleic acid carries an “instruction manuel” to produce proteins that are responsible for passing traits from your parents to you. As you demonstrated in the previous activity, deoxyribonucleic acid is made of four nucleotides base pairs: adenine, thymine, cytosine, and guanine. They are often abbreviated as A, T, C, and G. The uniqueness of deoxyribonucleic acid is not particularly in just these 4 subunits, but how they are arranged. In this activity you will recreate protein synthesis.

We did this to test which test tube would contain the highest concentration of glucose. What we wanted to know was if the lactase would affect the function of the enzyme. Our hypothesis is the lactase functions within a narrow pH and that will change in pH would affect the function of the enzyme. We predict that if we change the environmental factors it will have an effect the function of the enzyme if the pH is outside the range in its optimum activity. Our hypothesis was then proven because the reaction only occurred in a neutral and acidic state of pH, not basic. Which means the enzymes prime ability to function is a neutral, and acidic pH range.

Organisms cannot depend solely on spontaneous reactions for the production of materials because they occur slowly and are not responsive to the organism's needs (Martineau, Dean, et al, Laboratory Manual, 43). In order to speed up the reaction process, cells use enzymes as biological catalysts. Enzymes are able to speed up the reaction through lowering activation energy. Additionally, enzymes facilitate reactions without being consumed (manual,43). Each enzyme acts on a specific molecule or set of molecules referred to as the enzyme's substrate and the results of this reaction are called products (manual 43). As a result, enzymes promote a reaction so that substrates are converted into products on a faster pace (manual 43). Most enzymes are proteins whose structure is determined by its sequence of its amino acids. Enzymes are designed to function the best under physiological conditions of PH and temperature. Any change of these variables that change the conformation of the enzyme will destroy or enhance enzyme activity(manual, 43).