Enzyme Kinetics Laboratory Report

Enzyme Kinetics Laboratory Report How the changes in substrate concentration (PNPP), changes in temperature, changes in pH and the presence of an inhibitor (phosphate ions) effects the rate of reaction of the reaction between PNPP and water catalysed by the enzyme acid phosphates which produces PNP and phosphate as its products . Using spectrophotometer to measure the absorbance of the products formed through hydrolysis of substrate. Abstract: The purpose of this scientific paper was to replicate earlier findings of experiments in enzyme kinetics and to see if enzyme behaviour and activity is influenced by 4 factors- change in substrate concentration, temperature, pH and the presence of a competitive inhibitor. In the first section where the substrate concentration was altered whilst the enzyme concentration was kept constant the relationship was found to be hyperbolic this can be explained using the Michaelis -Menten equation and the Lineweaver burk plot which was also used to obtain Km values of 0.25 and Vmax values of 0.12UNIT. The increase in [S] increased the rate of reaction at first but when [S] too much the initial velocity started to decrease. The increase in temperature led to a general increase in the initial velocity until the temperature reached 347 K where the enzyme denatured. The optimum temperature of the reaction was in the range 310 K- 323.2 where the rate increased at its fastest. The third section was the effect of pH on the enzyme activity. The optimum pH of the reaction was 5.5. This pH gave the highest reading of absorbance which means that the rate of hydrolysis was at its highest. Finally the last section of the experiment was the effect of competitive inhibitor on the rate of reaction. The investigation showed that the inhibitor used (phosphate ions) was a non-competitive inhibitor. The inhibitor did lower the initial velocity of the reaction when it attached to the enzyme at random. Introduction: This laboratory report is on the topic of enzyme kinetics, previous work in this particular field was carried out in the 1700s, when biological catalyst enzymes were discovered and studied. As understanding of enzymes increased scientist carried out basic laboratory experiments such as the conversion of starch to sugar by saliva to increase their understating of enzymes and how they function. However the first actual incident where enzymes were understood in detail was in 1897-by Edward Buchner .Since then on, till this period of time factors which effect the velocity/ rate of reaction and enzymes have been studied widely by many scientists globally. The modern scientists have a deep understanding of enzyme kinetics. The purpose of this laboratory report is to confirm previous findings covered in various sources of scientific literature and journals. Enzymes are often described as organic catalysts which increase the rate of reaction of a bio-chemical reaction ( David L.Nelson etal 2008). Enzymes increase the rate velocity of various reactions that occur in a biological system such as the mammalian digestive system. Enzymes can have functions including transfer, synthesis or breakdown of molecules. It is important to mention that enzymes are proteins which speed up the rate of reaction without being used up themselves i.e. they are reusable. Enzymes have a very specific active site which is complementary to a specific substrate 3 dimensional structure. The specificity is due to the complementary hydrophilic/hydrophobic charge, electrical charge and shape of active site on the enzyme. The binding of an enzyme with an specific substrate produces an enzyme substrate complex (ES).The rate at which the enzyme substrate complex is formed is dramatically increased or decreased in changes in substrate concentration, temperature, pH and presence of an competitive inhibitor the effect of these 4 factors on the enzyme activity is known as enzyme kinetics (Jeremy M. Berg etal 2006).Enzymes work on the concept of transition states. Transition state of enzymes is the phase where the substrate is not a yet a product and not a substrate. Enzymes reduce this phase .The difference between the free energy of the reactants and the free energy of the transition state is the activation energy (Ea).The minimum energy required for a success full reaction to occur. Enzymes speed up the rate of reaction by lowering the activation energy barrier. A typical enzyme substrate reaction can be simplified and be written as: The enzyme studied in this investigation was acid phosphatase. This enzyme can be identified by its Enzyme Commission Number (EC number) which is 3.1.3.2. Now I will briefly discuss the enzyme kinetic properties of acid phosphatase. The enzyme acid phosphatase catalyses the removal of phosphate group from organic molecules. Its primary mechanism of action is to bring a substrate molecule into contact with a molecule of water .This results in catalysis and the removal of phosphate group. Finally an hydroxyl group is attached to the substrate molecule. An example of this is the reaction shown below. This reaction was studied in this laboratory investigation. Acid phosphatase p-nitrophenylphosphate (PNPP) + water phosphate + p-nitrophenol(PNP) In the reaction above PNPP is the synthetic substrate, which is described as chromogenic.At. At high purity this compound is completely colourless. PNPP is hydrolysed by the enzyme acid phosphatase this produces phosphate and PNP. The product produced is yellow and can be measured using a colorimeter. The first part of the investigation concerns the effect of substrate concentration on the rate of reaction. I predict and expect that at an increase in substrate concentration (PNPP) will lead to an increased rate if reaction/initial rate. The reason for this is that an increase in substrate concentration increases the chances of a successful collision occurring between the enzyme and substrate increasing the likelihood of ES complex and product (PNP) formation results in an overall increase rate of reaction. This will produce a fist order reaction on a graph. However it is important to mention that at high substrate concentration the enzyme will be fully saturated this will reduce the rate of reaction as the there are too many substrate than enzymes. On a graph this would show a plateau. The maximum velocity of the reaction or the Vmax would be expected to be close to this region. Therefore I predict to see a hyperbolic relationship on a graph. Section B of this investigation concerns the effect of temperature on the rate of reaction. I would exepcet to find that an increase in temperature would result in an increase in the rate of reaction. The reason for this phenomenon is that as there is increase in kinetic energy being applied to enzymes and substrates it increases the chances of collision occurring so more product (PNP) is formed per unit time. However I also believe that temperatures above 50 -70 degrees Celsius would denature the enzymes active site and the 3 dimensional structures. At this stage the enzyme will not be complementary in shape to the substrate. This would mean that no reaction can be completed so the rate of reaction will decrease. It is important to state that the enzyme is going to have an optimum temperature at which the ES complexes and products are made at the fastest velocity. The increase in temperature increase the amount of molecules which have higher energy than the Ea barrier this in turn increases the amount of molecules which can react increasing the rate of reaction or initial velocity. I believe the optimum temperature is going to range between 20-40 degrees Celsius. The third part of this lab report is based on the effect of pH on the rate of reaction again I believe that at extremes of pH such as acidity or alkalinity will affect the rate of reaction. This may cause the enzymes structure to denature and will cause a lower rate of reaction and lower rate of product formation because the enzyme will not be complementary to the substrate. I would expect this enzyme to have a low optimum pH of around 5-2 as it is acid. Finally the last section of this investigation concerns the effect of a competitive inhibitor (phosphate ions) on the rate of reaction. Inhibitor in this case the phosphate ions will compete with the actual substrate PNPP for the active site of the enzyme acid phosphatase. These inhibitors can only attach to the active site of the enzyme due to their complementary properties. The concentration of the inhibitors will be kept constant and the concentration of the substrate PNPP will be altered. I believe that as the concentration of PNPP increases the rate of reaction will increase this is because the PNPP can out- compete the competitive inhibitor and reverse the effect of the inhibitor. Materials and Methods: All procedures were carried out as described in the lab schedule. No alterations were made to any of the procedures carried out throughout the experiment. Discussion: The first section of this lab report relates the effect of substrate concentration on enzyme activity. I shall briefly discuss and explain what my data shows and means. Graph 3 which is the graph of Michaelis Menten of collected data. The relationship between the rate of an enzyme-catalysed reaction and the substrate concentration can be describes as hyperbolic. The graph and tables 2 show that as the concentration of substrate (PNPP) increases from 0.00 Mmols to 0.20 Mmols of substrate the initial velocity or the rate of reaction shows an increase in too. The relationship can be describes as fist order as the [V] rises almost linearly with the increase in [S]. However after the concentration increase from 0.20- to 3.00 Mmols the initial velocity shows a gradual increase and then gradually levels of or slopes here graph shows 0 order relationship. This supports the prediction I made in the introduction. The graphs indicates that as the concentration of substrate increase the rate of reaction increase this is because of the increase chances of a collision between a substrate and an enzyme. This in turn increases the rate at which ES and P are formed. However after the concentration increase after 0.20 3.00 Mmols the rate stars to level off. The reasoning behind is this is that there are too many substrates than compared to enzymes an all enzymes are described to be fully saturated .At this phase the reaction is at its Maximum velocity and cannot increase in rate unless more enzymes are added therefore enzyme concentration is the limiting factor. I can tell that the data I collected from the experiment in the lab is accurate and valid as the graph which compares the theatrical data and the collected data show similarities in the trend line the Vmax the km and as well as the points and there is no anomalous data point on either of the 3 graphs. My findings support the findings of many previous investigations and journals as the graphs show a similar relationship as to the findings to previous work. The implications of this investigation can be used widely to determine the Vmax and KM. These values can be used for medical purposes since the enzyme acid phosphatase is manufactured by the body to remove phosphate groups. The limitation of Michaels Menten plot is that the Km and Vmax cannot be accurately determined. Therefore a Lineweaver burk plot is plotted. The Lineweaver burk plot shows that the KM and Vmax are very similar to the ones from the Michaelis Menten plot. Finally KM is an approximate measure of the affinity of an enzyme for its substrate.A small value of KM indicates a high affinity of the enzyme for the substrate. From my graphs (1 +2) I can tell that the KM was 0.24 and therefore small. This means that the enzyme acid phosphatase has a high affinity for the synaesthetic substrate PNPP. This means that small concentration of substrate PNPP is enough to run the reaction at half of maximum velocity (1/2 Vmax). The next section of the investigation concerns the effect of temperature on the rate of reaction. I predicted an increase in temperature will increase the rate of reaction or the initial velocity of the e reaction until the enzyme denatures and the protein sequence becomes damaged an unravels. The actual reason for why the protein sequences unravel is that the protein has too much kinetic energy and the amino acids vibrate and this causes the non covalent forces to be weakened. There is an increase in the rate of reaction as the temperature increases from 278 -323 K the increase is almost linear. However after the temperature 323 K-to 347 K the enzyme denatures and unravels. This is proved by the last point on the graph which doesnt fit the line of best fit. Overall the graphs and data all prove my predictions correct. There is no other anomalous data present. The third section concerns the effect of pH on the rate of reaction. As we have discovered before the enzyme used was acid phosphatase so the pH at which it works at best the optimum temperature will be in the acidic pH regions. I can confirm from my graph that the optimum pH of the reaction is in the region 5-5.5 which is indeed acidic. pH of 5.5 gives the highest absorption value, this therefore means that the rate of hydrolysis was at its fastest. A possible explanation for the change in the experimental design is that the pH may denature the enzyme if the enzyme was added first the active site and 3 dimensional shape of the enzyme could be altered at extremes of pH such as 2 which is quite acidic. The pH does not affect the substrates 3 dimensional structure in the same ways as the enzymes. Therefore to obtain valid results /data the design for this part of the experiment was slightly altered. pH has a very strong effect on enzyme activity .This is because enzymes work on the basis of mechanisms such as induced fit hypothesis and lock and key . The enzymes have a specific active site due to the complementary 3 dimensional active site with the substrate. According to the induced fit hypothesis the enzyme can undergo some change in the 3- dimensional structure in order to fit the substrate. However a change in pH changes the enzymes active site structure. An increase in H+ ions can change the active site structure due to the fact that h+ ions can interfere with any polar molecules on enzymes protein structure. Amino acids side chains can be protonated and may be damaged due to the extreme pH (concentration of H+ )this may result in the protein sequence to unravel which means that the active site is not complementary to the substrate and the rate of reaction decreases as no or little ES are formed which results in little products formed. The final section concerns the effect of a competitive inhibitor (phosphate ions) on the rate of reaction. From my graph I can tell that the inhibitor present was an non-competitive inhibitor. I can tell this by looking at the Lineweaver Burk plot where the trend lines cross the 1/Vmax intercept at different values but cross the 1/km intercept at the same values. This means that this type of inhibitor does not affect the KM but does lower the Vmax values. Non competitive inhibitor has the same effect as lowering the total volume of enzyme. This type of inhibition is reversible. It binds to a site away from the enzymes active site it denatures the active site so no other substrates can bind to the active site. This in turn lowers the rate of reaction and the rate at which products are formed. However this type of inhibitor also binds to the enzyme substrate complex I can therefore conclude that the non competitive inhibitor does lower the rate at which the products are formed. References: Books: David L. Nelson et al (2008) Lehninger Principles of Biochemistry ,W.H Freeman and Company Jeremy M. Berg et al (2006) Biochemistry, W.H Freeman and Company Lab schedule (2009) Enzyme Kinetics MODULE LSC10034 EXPERIMENT 4 Lecture Notes: Lectures notes (2009) Dr John Mills- Module LSC-10034 Proteins and Enzymes lectures 9, 10, 11 (Figures 1-5) Absorbance values- Table 4 and Table 6 Emma Ezekiel Web Pages: EC Number -http://www.brenda-enzymes.org/php/result_flat.php4?ecno=3.1.3.2 Seen :20 November 2009

Collaborating to Expand the Pipeline Essay

                  Affirmative action is a policy that is aimed at providing positive measures to remedy effects of past discrimination against members of certain groups (Clayton & Crosby 1992, p.2). One of the areas that suffer underrepresentation of the diverse, underrepresented individuals and minority group in colleges is the laws schools and subsequently in the legal profession. The questioned posed is â€Å"Is affirmative action the best solution to alleviating this crisis or is it the major cause together with other practices that have contributed to these underrepresentation?                     First of all is the admission procedure. Admission selection considers those with a bachelor’s degree for an accredited university or college. Few underrepresented minority students are able to attend college and obtain the relevant qualifications. Moreover, there are disparities in number of applicants and the number who get enrolled. For example in 2000, 74500 individuals submitted their application to ABA- approved school and an estimate of 67% of the total were admitted (ABA/ LSAC Pre-Conference Report, 2005, p, 4). This illustrates a flaw in the acceptance procedure that focus on higher merit in which its well document trend that underrepresented minorities score less on the Law Schools Admission Test (LSAT).                   Secondly the individual state bar exams are a severe impediment. â€Å"While the LSAT remains a reliable predictor of success in law school and the Law School Admission Council (makers of the LSAT), warn against over-reliance on numerical qualifiers alone† (ABA/ LSAC Pre-Conference Report, 2005, p, 5). Raised cut off points detriment the minorities who are disproportionately at the bottom in addition the bars are also misapplied. The percentage of residents in a state should have a proportionate percentage at the law school. The lack of a national bar does also contribute to this issue.                      The above two examples illustrate why affirmative action is needed in leveling admissions. Higher merit and higher cut off points are serving to lock out minority groups from accessing law education. In coming up with a criteria for selection, the selection board should put into consideration performance of minority groups which is at the lower end of the spectrum.                   Terry Eastland suggests that affirmative action promotes discrimination. He argues that there is nothing like positive or negative discrimination. In Higher education for example, when the institution sets a lower grade for color students, the act in itself creates discrimination. These groups of students who will be enrolled under affirmative action are well aware that they are in that position due to their race. It is a negative experience that is not easy to erase. Sometimes attitudes from the majority students will affect the students from the minority. The majority students may not look at the minority as equals.                   Affirmative action leads to stigma. Eastland says that very few people are aware of the abilities and potential of the marginalized groups. In this case they are likely to be less respected and less valued. This can end up psychologically affecting these groups and it can be worsened if they fail to perform. Terry end believes that an environment should an equal working basis. If students have to be enrolled for higher education, it should be based on merit and not race. This will create an equal working environment of mutual relationship.                  Furthermore, Eastland equates ‘Affirmative action’ to ‘lower standards’. The rationale of having a policy that sets asides positions after a normal criterion creates a barrier between quality and less quality. By having this policy, institutions are accepting that results posted from minority groups are of lesser quality and lesser magnitude to that from the majority. Policy makers argue that the minority are affected by certain factors that make them not to equal results of the majority. It then beats logic that it would be easier resolving factors that make minority perform lesser than providing a criterion that guarantee certain results.                  Terry Eastland comments and views in regard to affirmative action tend to disapprove use of affirmative action against underrepresentation based on color. His views do not factor underrepresentation due to gender. However the logic behind his reasons and those of other scholars can equally be equated to affirmative action on gender and sex segregation                  Gender affirmative actions have shown to improve the status of women in the society. In fact advocates for gender affirmative actions have sprung from various women activists and organizations. Women have gained access to representations in legislative organs, various courses in colleges that stereotypically were set for men. However it is urged that continuous paying attention to a group of people will result in then differences becoming more salient than the commonalities among people (Clayton & Crosby 1992, p.11). This statement thus emphasizes Terry Eastland’s arguments against affirmative action.                To conclude, the benefits of affirmative action are actually visible. Moving forward however, the fundamental principles of affirmative action seem to have been overtaken with time. Putting into consideration Terry Eastland arguments in regard to affirmative action, the negatives of affirmative action outweigh the positives. Affirmative action has led to lower productivity, increased segregation and stigmatization. The call to end affirmative actions thus is justified. References Clayton, Susan D, and Faye J. Crosby. Justice, Gender, and Affirmative Action. Ann Arbor, Mich: Univ. of Michigan Press, 1992. Print. Law Schools Admission Council. Pre Conference Report (2005) Collaborating to Expand the Pipeline. Retrieved from http://www.americanbar.org/content/dam/aba/migrated/op/pipelineconf/PipelinePostReport.authcheckdam.pdf Source document

Communication Satellite Corporation Essay

The following judgment on the appropriate economic regulations of the Communications Satellite Corporation (Comsat) has been arrived at after considering the due deliberations presented before the Commissioners by the two parties; namely Comsat and FCC. Central to this judgment is the premise that â€Å"the return to the equity owner should be commensurate with returns on investments in other enterprises having corresponding risks.† Also, the fair rate of return should be actually that required (or expected) by a firm’s investors. The Commissioners are also of the view that the interests of the ratepayers should be safeguarded. The ratepayers should not be penalized for any change in circumstances (e.g. excess liquid cash due to change of technological needs) resulting in inefficiency at Comsat. Such risk should be borne by the Shareholders alone. The judgment covers the fair rate of return awarded to Comsat (commensurate to its risks), the rate base and the price structure to be followed by Comsat. At the onset, we concur with Comsat’s argument that their risk profile cannot be compared to that of AT&T due to the following: 1. Even though AT&T is in the same business of providing communication channels, yet the equipment used is vastly different i.e. satellites versus data cables. 2. AT&T is a well-established utility while Comsat is a new venture. Their risk profiles are not similar. 3. Considering the testimony of Dr. Myers, the beta found for AT&T and Comsat are different thus implying that the investors view the inherent risk of the companies differently. Next, we look into the various risk factors discussed before us in order to reasonably estimate the risk inherent in Comsat. Operating Risks 1. Technological Risk: The trial staff established low technological risk by considering in hindsight the fact that Comsat’s evolution was relatively trouble-free. In our opinion, this is unjustifiable as when the company was started there was no way of knowing this and the technological risks were immense. 2. Business Risk: There was no government guarantee for Comsat. Also, considering the fact that disclosing information in a prospectus in no way changes the risk associated with the business. 3. Demand Risk: The arguments put forward by the trial staff in this case are sound but do not present a case for comparison with AT&T. 4. Competitive Risk: We think that competitive risk is medium, thus deviating from both the trial staff and Comsat’s stand. This is because although high risk was created due to Comsat’s competitors being its customers, it was also mitigated to some extent by FCC’s support. 5. Regulatory Uncertainty: Again this uncertainty of prospective regulation is reduced by expected support from FCC. 6. Political/International Risk: We agree here with the trial staff’s response. The risk faced by Comsat is probably just a little greater than that faced by other international organizations operating in those countries during that time. From the above discussion, we conclude that the company faces more operational risk than that touted by the trial staff albeit it is not as high as Comsat claims. Financial Risk The trial staff wants to impute the implications of a 45% debt structure to calculate the cost of capital. This is incorrect since firstly, there were no assets that could be used as security till 1972 and secondly, this is a hypothetical situation of which there can be many. However, we are of the opinion that the debt should be imputed at a rate of 45% post-1972 as a miscalculation on part of the management should not result in unjustified price structure for the ratepayers. Rate Base The appropriate rate base should now be calculated based on the above decision to impute debt post-1972. Pre-1972, the rate base will be the entire capital of the company. Evaluation of Cost of Capital We disagree with the first two witnesses, namely Dr Brigham and Dr Carleton and their estimation of Comsat’s cost of capital. Dr Brigham’s method takes into account 602 industrial firms and 56 utilities. These two categories of companies are not comparable for the purposes of this analysis. Also, the Andersen study using four utilities and its results is not worth considering since these utilities had a different capital structure and consequently, a completely different risk profile from that of Comsat. Dr Carleton has arrived at a risk premium of 2-4% but has provided no reasonable justification or methodology followed for calculating this. Also, we have no indication whatsoever about the nature of this premium, whether it is the risk premium for Comsat or the utilities sector or the market or the country as a whole. We concur with Dr Myers’ methodology of using the CAPM for calculating the risk premium. This study further simplifies matters as the cost of equity and the cost of capital is the same for this firm pre-1972 and incorporate the cost of debt post-1972. Also that the beta in this case would be calculated on the basis of market data. Assuming the markets to be efficient  implies that the appropriate risks have been implicitly factored into the prices and the beta. Based upon these estimates we will state the cost of capital to be 14%, which is the mid point found for the various risk estimates over time, taking into account a beta range from 1.4 – 1.7 as recommended by Dr. Myers. Pricing Structure The commissioners are of the view that Comsat was injudicious in charging the maximum rates the markets could bear. Instead, Comsat should have charged rate of return that is sufficient for it to maintain: a) to cover cost of capital already committed to the enterprise over and above the operating expenses incurred; and b) to attract additional capital as needed in competitive money markets at reasonable costs. We instruct FCC and Comsat to calculate the appropriate revenues for Comsat in line with the preceding judgment. Comsat should be penalized 50% of the excess revenue, if any, and FCC should use this money to further infrastructure development in Communication systems.

How To Tame A Wild Tongue Summary - 999 Words

A few months ago, in Charlottesville, Virginia, a young women named Heather Heyer, was killed at a protest against a white supremacy rally. She was standing up for others who were different then her. She was making sure her fellow citizens felt welcomed and knew they were loved by others in this country. This happened less than two hours away from Lynchburg, our home. We, as a nation, need to start embracing one another because at the end of the day, we all bleed the same blood. My wish is that one day we can all live together in peace. It starts at home. We have to begin a dialogue with our friends and family about the struggles others go through. Accepting one another is so much deeper than simply saying, â€Å"I support you†, although thats†¦show more content†¦A group of individuals trying to take away someone else’s freedom of expression, trying to make this country divide even more. Gloria talks about these divisions all throughout her story. Certain peo ple groups are taught at a young age, that if someone looks or sounds different then you, they shouldn’t be welcomed in this country. Trying to take away or restricting someone from certain rights because they’re different from you is illegal. This can also go back to Gloria’s quote about attacks on the first Amendment. Everyone that is a citizen has the right to feel safe in this country and has the right to express their beliefs. Accents are one of the many things that make us different. As a free country, we should embrace them not suppress them. Some groups of individuals still, to this day, hate others because of their skin tone or language they speak. I personally think that those people are jealous and wish they could speak that way or share the culture. To me, each and every culture in this world is beautiful. The way they speak, the way they dance, the way they sing, and the way they dress, are all beautiful. For native english speakers we are taught in school that we have the most superior culture in the world, but that is statically wrong. Today, Chinese (more specifically mandarin) is the most common language spoken, according to Babbel.com. Can you imagine what it would feel like for you to goShow MoreRelatedHow to Tame a Wild Tongue1952 Words   |  8 Pagesâ€Å"My Perspective of a Wild Tongue† â€Å"How to Tame a Wild Tongue†, by Gloria Anzaldua, is a very expressive story about a Mexican American women’s struggle to preserve her culture. Her main fight revolves around a struggle to keep a form of Spanish, called â€Å"Chicano Spanish†, a live. In the short story she says, for a people who cannot entirely identify with either standard (formal, Castilian) Spanish, or standard English, what recourse is left to them but to create their own language?(pageRead MoreRn Language1591 Words   |  7 Pagesprofession, as well as the importance of maintaining these elite level communication skills. 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