Beta Secretase Research Paper

Hold the IKI spray bottle 25 - 30 cm away from the paper towel, and mist with the IKI solution.

Enzymes are the very successful machines of natural life. They are in charge of lowering so as to catalyze responses the enactment vitality for these responses. Enzymes are comprised of proteins interpreted from nucleic corrosive coding material, so they have particular duties inside of a life form. Beta-lactamase is a enzyme that separates beta-lactam anti-toxins like penicillin. In this lab, the viability of the beta-lactamase catalyst was tried at diverse temperatures. The beginning speculation of the trial was that enzymatic action would increment as temperature expanded, in spite of the fact that at 60 degrees Celsius the chemical would denature. This was somewhat reflected in the information. The chemical did denature at 60 degrees; in

Determining the Production of Glucose During Changes in Temperature and pH, and Manipulation of Specificity and Cofactors

The specific enzyme beta-hexosaminidase A is responsible for catalyzing the biodegradation of acidic fatty material in the brain and spinal cord known as gangliosides.

Alzheimer’s Disease is indicated by the break down of the nervous system, essentially the neurons within the brain (MacGill, 2009). The break down leads to nerve cell eradication, and the casualty of tissue throughout the brain (MacGill, 2009). As the disease progress, the brain begins to shrink fiercely, developing loss of its normal functioning (MacGill, 2009). Abnormal protein groups and structures of plaques and tangles characterize the disease (MacGill, 2009). Plagues and tangles are not able to be viewed or tested in the living brain, but are able to be observed in an autopsy of an infected deceased (MacGill, 2009).

Enzyme Lab Report Jessica 9B RESEARCH QUESTION What is the effect of different concentrations of catalase on the rate of reaction? BACKGROUND RESEARCH The task of an enzyme is affected by many factors.

It would be the amount of substrate (penicillin G) that would vary in increasing amounts in each test tube. One test tube will have no substrate with each tube having more substrate than the other until there is a lot of substrate.

Although there is presently no cure for MS, modern research has developed several medications and other treatments that slow the course of the disease and help patients cope with its symptoms. Steroids shorten acute MS attacks by reducing inflammation in the nervous system, but they do not help prevent relapses or slow the overall progression of the disease. Betaseron and Betaferon, different brand names for interferon beta, have only been available since 1994, so doctors do not yet know what the long-term effects are. Clinical studies show that the drug reduces the frequency and severity of MS attacks in about two-thirds of the people who take it. It also reduces the number of new areas of demyelination. Interferon beta seems to work well on relapsing-remitting and secondary-progressive

There is a large supply of amyloid plaques in the cells of people with Alzheimer’s disease. Amyloid plaques are clustered pieces of protein that build up between nerve cells. They speed up the production of beta amyloid, which are polypeptides of about thirty-six to forty-three amino acids long (emedicinehealth, 2014; Stanford Medicine, 2013). Amyloid precursor proteins (APP), when split into specific pieces, are producers of beta amyloid. They are found in tissues and organs, such as the brain. Amyloid precursor proteins pass through a fatty membrane on the outside of a cell. This allows them to extend from the

Alzheimer’s disease is the most common cause of dementia, affecting over 40 million people worldwide. Yet, finding a cure is something that still alludes researchers today. Dr. Alois Alzheimer, a German psychiatrist, first described the symptoms in 1901 where he noticed that a particular hospital patient had some peculiar problems, including difficulty sleeping, disturbed memory, drastic mood changes, and increase in confusion. When the patient passed away, Alzheimer was able to do an autopsy and test his idea that, perhaps, the patient’s symptoms were caused by irregularities in the brain’s structure. What he found beneath the microscope were visible differences in brain tissue in the form of misfolded proteins called plaques and neurofibrillary

PSEN1 and PSEN2 are polytopic membrane proteins (Davis et.al., 1998) that form the catalytic core in the protease γ-secretase (Francis et.al., 2002), which is responsible for the proteolysis of APP (Navivaeva & Turner, 2013). When there is a mutation at the loci for PSEN1 and PSEN2, located on chromosome 14 and 1 respectively, the activity of γ-secretase is altered resulting in changes in the proteolysis of APP and increased formation of Aβ (Qain et.al., 1998). Due to the increase of Aβ, amyloid plaques aggregate quickly causing early-onset of AD.

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).

Amylase is an enzyme that is located in human saliva. It is solely accountable for breaking down starch as a way to start the breakdown of food and is one of the first steps of digestion. The time at which the enzyme starts the chemical reaction with starch is called the reaction rate. In order to study how amylase works against starch, this experiment consisted of two tests; each testing a different condition of amylase. The first test was to simply study the reaction between saliva and amylase and note the reaction rates. The second test was to see if increasing the pH would decrease the reaction rate or halt it all together. Saliva was collected, diluted, and tested for reactions between starch and amylase. Another sample of saliva was collected, diluted, and had its pH increased and tested for reaction rate. The findings after the experiment was conducted aligned with the original hypothesis. The change in pH did show a significant decrease in the reaction rate.

The purpose of this lab report is to investigate the effect of substrate concentration on enzyme activity as tested with the enzyme catalase and the substrate hydrogen peroxide at several concentrations to produce oxygen. It was assumed that an increase in hydrogen peroxide concentration would decrease the amount of time the paper circle with the enzyme catalase present on it, sowing an increase in enzyme activity. Therefore it can be hypothesised that there would be an effect on catalase activity from the increase in hydrogen peroxide concentration measured in time for the paper circle to ride to the top of the solution.

In this lab we looked at the role of pancreatic amylase in the digestion of starch and the effect that temperature and pH has on this enzyme. Enzyme’s work as catalysts that increase the rate of chemical reactions within cells (Cooper, 2000). In order to do this, enzymes must show two essential properties: these two fundamental properties of enzymes include increasing the rate of chemical reactions without being eternally altered by the reaction and accelerating the reaction rate with keeping the reactants and products in chemical equilibrium (Cooper, 2000). Enzymatic catalysis is necessary for life. Most biochemical reactions would not occur under the mild temperatures and pressures