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    Investigating the Best Temperatures betweem Calf Trypsin and Fugal Trypsin PROBLEM BEING INVESTIGATED BACKGROUND Trypsin is an enzyme so to be able to conduct a suitable plan, this idea will help me to predict the best temperature that can be achieved on its activities in different conditions. “Collins Advanced Science Biology defines an enzyme as biological catalysts, speeding up reactions that would otherwise happen too slowly to be any use to the organism, that is it has catalytic

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    §     Photographic film (b/w) §     Syringe §     Test tube rack §     Ruler §     Scissors §     O.1% trypsin made in pH7 buffer solution §     Mounted needle 2.     I then decided on the range of results and temperatures I was to investigate. I decided to observe 20º, 30º, 40º, 50º, 60º, 70º and 80º. 3.     Next, I label each test tube with the temperature to be investigated and then added 2.5cm3 of Trypsin solution. 4.     I ensured that I cut the necessary pieces of film using a ruler and a pair of

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    Investigation on the Enzyme Trypsin An Investigation determining a factor affecting the rate of digestion of gelatin by the protease trypsin. Introduction An enzyme is a biological catalyst, which speeds up reactions. An example of this in the human body is trypsin (a protease produced in the pancreas and used in the stomach), which catalyses the digestion of gelatine, a protein. For this investigation, a photographic film will be the source of the gelatine. I will be able to identify

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    Pepsin Vs Trypsin

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    that they had a defined structure It is the first animal enzyme to be discovered, and was named after the Greek word peptein means to digest. Pepsin is one of three important proteolytic enzymes in the system, the other two are chymotrypsin and trypsin. The main function of proteolytic enzymes is to help in hydrolysis of proteins into peptides and amino acids by

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    pH for trypsin is 8, then reactions occurring in environments above or below will result in lower proteolytic activity and thereby slow reaction rates.” After testing several pH’s 5, 7, 8, 9, and 11 it is impossible to fully accept or reject our hypothesis that we set especially using the rationale about trypsin in the small intestines. By trypsin being located in the small intestines where the pH is 8 one would believe that any other pH whether above 8 or below 8 would cause for trypsin to have

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    Investigation into the Digestion of Milk by Trypsin Background Knowledge ==================== To investigate the effect of trypsin on milk a number of separate experiments will be performed whereby milk is digested by trypsin under controlled conditions. Specific variables will be changed by calculated amounts to gauge their individual effects on the rate and amount of reaction that occurs. Trypsin is a biological catalyst, (a substance that speed up a reaction without being used

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    The Effect of pH on the Digestion of Casein by Trypsin When planning the experiment, the equipment and method had to be well thought-out in order for the experiment to be accurate and efficient. Firstly, I have chose to use a 1% trypsin concentration then altered it to 0.8%, because a higher concentration means more trypsin molecules in the solution and therefore more enzyme substrate complexes are likely to occur with the casein in the milk, causing digestion of the casein to be faster

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    The Factors that Affect the Rate of Breakdown of the Protein Gelatine by Trypsin Aim To investigate factors that affects the rate of breakdown of the protein gelatine by trypsin. Key Factors: Possible factors that I could change- pH- Different types of enzyme work best at different pH level. The best pH level for an enzyme to be effective depends on its site of action. An example of this is; enzymes in the stomach have an optimum pH value of about 2. This is because the stomach

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    accomplish this. Trypsin, the enzyme being studied in this project, is one such enzyme. It is separated into two categories: early trypsin, which appears shortly after a blood-meal, and late trypsin, which appears later in digestion, and which does most of the work of digestion. The project found evidence that early trypsin activity (that is, the presence of early trypsin in the gut following a meal) was essential to the production of late trypsin later in the experiment. The early trypsin is present in

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    Zymography Essay

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    There are various types of zymographic methods. They are substrate zymography, Gelatin zymography, Casein zymography, Collagen zymography, Heparin-Enhanced Substrate zymography, reverse zymography and in situ zymography. Zymography is considered as a standard technique to examine the activity of enzymes involved in the cellular processes[87]. Gelatine zymography is an efficient and sensitive method compared to other methods to detect both pro- and active form of proteins [88]. Reverse zymography

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    fats and aid in increasing lipid digestion rate. The pH of the environment in our digestion tract also affects digestive enzymes since they are more effective at certain pH levels; for example, pepsin is more active in acidic environments whereas trypsin works more effectively in basic conditions. Before this lab, I did not realize how pivotal pH environment is to help digestion. I also learned that another factor that helps aid in increasing the rate of digestion is increasing the surface area of

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    protein was finally digested by the use of trypsin. Protease trypsin cleaved peptides on the C-terminal side of arginine (R) and lysine (K) residues. If a proline (P) residue is on the carboxyl side of the cleavage site, the cleavage would not occur. The digestion parameters are listed in table 1. The first parameter was setting trypsin as the protease because trypsin was assigned. The program was set to have a maximum number of missed cleavages of 1 because trypsin has high activity and narrow specificity

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    typically large, rigid molecules 2-3 polar groups, and easy to dock to. Perfect sampling and high scoring success is observed in almost all the 47 complexes in this family. Complexes with the native substrate include estradiol 1QKT, 1QKU, 1A52. Trypsin is a serine protease found in the small intestine. It has a highly charged binding site with a triad of three catalytic residues His57, Asp102 and Ser195. There is a Calcium ion in the binding site. A large amount of crystallographic data is available

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    pancreatic enzymes are: pancreatic amylase which breaks down starch to maltose, trypsin which breaks down proteins into polypeptides and amino acids and pancreatic lipase which breaks down fat into fatty acids and glycerol. Trypsin is secreted as an inactive precursor trypsinogen. This is converted into trypsin by the action of the enzyme enterokinase, secreted from the wall of the small intestine. The products of amylase and trypsin digestion cannot be absorbed but the fatty acids and glycerol can be. Pancreatic

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    I finally quit smoking after 30 years, after my doctor told me that I wouldn’t see my kids graduate if I continued to smoke. Initially, it was torture for me. I would often have headaches and nausea, which resulted in me being irritable all the time. However, after a few months, those symptoms disappeared. I thought that for once, I finally got past my dark history of smoking. However, there were a few symptoms that still lingered. I had a cough that just wouldn’t go away, my lips would turn blue

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    Pancreas Essay

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    Protease breaks down protein into the building block form of amino acids. The three main proteases that it produces are: pepsin, trypsin and chymotrypsin (Marie, Joanne; Media Demand, “What Are the Functions of Amylase, Protease and Lipase Digestive Enzymes”). Pepsin does not occur in the pancreas but it is the catalysis in starting the digestion of proteins. Trypsin and chymotrypsin are the two proteases that occur in

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    Digestion – *There is no mastication or digestion of food in the bucco-pharangeal cavity. *The food passes to stoamach through the peristaltic movement of oesophagus. *The lumen of the oesophagus is kept moist and slippery with the help of mucous secreted by mucous glands. *The prey is captured by

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    Stem Cells and Parkinson's Disease

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    The goal of this paper is to compare the utility of adult, embryonic and induced pluripotent stem cells (iPSCs) to treat Parkinson’s disease. As such several things will be assessed, dosage of stemcells, improvement in motor function, in combination with the presence of α-synuclein proteins and cell survival. To give a short overview of the steps that will be taken to complete the study. Obtaining stem cells, whether adult, embryonic or induced, shall be done using healthy mouse models and after

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    Pomegranate Pomegranate is rich in antioxidants and has gained popularity as a healthy food. The health benefits of the fruit, its juice, and extract have been studied in relation to chronic illnesses, including cancer. • Prostate cancer. Pomegranate fruit and extracts have been shown to suppress each phase of prostate cancer by inhibiting proliferation, growth, invasion, and angiogenesis in human prostate cancer cells in vitro and implanted lab animals. Pomegranate juice was found, by Israili researchers

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    14, 15). Duct obstruction from pancreatic juice and its content increases pressure, leading to distension of the duct also (13, 14, 15). At a cellular level, membrane trafficking becomes chaotic, potentially leading to Trypsinogen activation into trypsin, initiating the cascade of digestive enzyme activation and autodigestion of the pancreas, causing AP (13,14, 15). Alcohol abuse further prompts acinar cells to release inflammatory cytokines, attracting a strong immune reaction causing pancreatic

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