Eurasian Watermilfoil and Exotic Species

Summary:   The invasion of Watermilfoil as an Exotic Species. I had to do this for a biology project.

Eurasian Watermilfoil
1. Exotic Species are often considered invasive or pollutants – why”

Exotic Species can be invasive or pollutant because they damage food webs, bring in diseases, and cause competition for food and nutrients.2. Describe how the organism spread to this non-native region.It is from Europe, Asia, and Northern Africa. It came here from boating activities as the milfoil stuck to the boat, and became transported into a new region.3. State the biome in which your organism lives, and describe the habitat.It lives in the grassland biome. It lives in lakes on the East Coast and Midwest. The Eurasian Watermilfoil infects ponds, lakes, streams, reservoirs, estuaries, and canals.4. Describe the organisms’ niche.Eurasian Watermilfoil has a type 2 niche, which means it always has an equal chance of survival. It can survive under ice, and in water with a pH between 5.4 and 11.5. What trends are they exhibiting in the environment in terms of population growth? Draw a model for this growth. Use a dotted line to project how the model will look after the next 100 years.There are not many ways to control the population of Eurasian Watermilfoil.

6. What limiting factors are present, what limiting factors are not present that are present in the organism’s natural environment”
Limiting factors include predators, parasites, high water temperatures, and plant quality. There are more predators in the natural environment.
7. What is the effect of this organism on the other populations in the ecosystem? What is the effect on the other species in that ecosystem”
What is the effect on the physical environment”
a) Fish can get trapped in the milfoil.
b) It can effect humans who swim near the Eurasian Watermilfoil by creating a rash.
Birds can transport the milfoil into other bodies of water
It can kill other plants by using nutrients and limiting growth of other plants.
c) When the plant dies, it releases phosphorous into the water. It also limits oxygen and sunlight to other plants underneath the water.
8. How does the issue of carrying capacity enter into the problem for your species? For the environment which includes other species”
Carrying capacity is not an issue for the milfoil. It affects other species because the growth of the Eurasian Watermilfoil can hurt the growth of other plants.
9. What has been done so far to deal with this problem”
A herbicide called Sonan has been used to kill the milfoil. Hand rakes have also been used for smaller areas. The cost to kill the Eurasian Milfoil is approximately one million dollars a year.
10. What solution do you propose and why”
I have two propositions. First, divers should pull out the milfoil manually. Second, I infected areas should be sprayed with chemicals such as Sonan or Fluridone to kill the Eurasian Watermilfoil to the root.
11. What are the drawbacks to this solution”
Pulling out the Eurasian Watermilfoil manually can disturb animals and plants that live on the floor of the water. Also, seeds could spread by manual work.
Killing the Eurasian Watermilfoil with chemicals can hurt other plants ability to photosynthesize.

Ethics of Posthumous Sperm Use

Summary:   Discusses the bioethical issues regarding the use of posthumous sperm. It also details the experience of a woman who has encountered this issue.

The request for retrieval of posthumous sperm is on the rise. Usually, the request is made by the wives of the deceased husbands. Ms. Nebel-Taylor was one of those women, who after her husband’s death insisted that the couple had been hoping for a child since before the illness. Mr. Taylor was hospitalized at New York Hospital when symptoms of what seemed to be a cold turned into severe shortness of breath and ultimate lung failure.

Nebel-Taylor claims she asked her husband, who was not ill then, what she should do if faced with such a dilemma. He responded for her to perform the procedure. When he later fell into a coma on a ventilator, Nebel-Taylor contacted Dr. Schlegel of the New York Hospital-Cornell Medical Center. She informed him of the situation, including the couple’s efforts to have a child and Mr. Taylor’s comment on sperm retrieval. Shortly after his death in 1995, a sperm specimen was removed from Taylor’s testicle by Dr. Schlegel, who in most cases refuses to perform this procedure. Ms. Nebel-Taylor proceded with in vitro fertilization during the year 2001, unlike most other women who never actually use the retrieved sperm. However, Taylor’s sperm was not viable. The only case of a child being conceived using posthumous sperm in the US was in 1999.Currently, there is no legal precedent regarding postmortem sperm retrieval. While some doctors believe in fulfilling the wishes of the wife upon grounds that the couple had been trying for a child, others hesitate when faced with arising ethical issues. As with Ms. Nebel-Taylor, physicians may call for thorough documentation proving the husband’s wishes for a child. However, most healthy young men rarely even address this issue. Problems may also arise if the man’s family opposes sperm retrieval, or if his parents request it instead of the wife in hopes of a grandchild. The child will also have to be raised by single parent and grow to question his or her own birth. Many women, nevertheless, believe that it is their right to decide whether to raise a child in this manner. In any case, bioethicists encourage family members to present documentation clearly stating the man’s wishes for a child, similar to that required for organ donation after death.


Summary:   A study of the effects of differnt enzymes on the rates of reaction. These effects are created through an experiment using the enzyme acid phosphates (ACP) and the substrate p-nitrophenyl phosphate.

Enzymes are an important part of all metabolic reactions in the body. They are catalytic proteins, able to increase the rate of a reaction, without being consumed in the process of doing so (Campbell 96). This allows the enzyme to be used again in another reaction. Enzymes speed up reactions by lowering the activation energy, the energy needed to break the chemical bonds between reactants allowing them to combine with other substances and form products (Campbell 100). In this experiment the enzyme used was acid phosphates (ACP), and the substrate was p-nitrophenyl phosphate.Enzymes are very specific in nature, which helps them in reactions. When an enzyme recognizes its specific substrate, the enzyme binds to the substrate in a region called the active site which is made of amino acids. Once the substrate binds, the enzyme changes its shape slightly to make an even tighter fit around the substrate, This is called induced fit and it allows for the enzyme to catalyze the reaction more easily. Another factor contributing to catalyses is the amount of substrate present; the more substrate molecules available, the more often they bind the active site. Once all of the enzyme’s active sites are occupied by substrate, the enzyme is saturated ( Campbell 99). Enzyme’s have optimal conditions under which they perform. These include temperature, pH, and salt concentration, amongst others. In this lab we only focused on pH and temperature. Each enzyme is specific to a certain optimal temperature and pH. When conditions are favorable, the reaction takes place at a faster rate, allowing for more substrates to collide with active sites of enzymes. However, if conditions get too extreme, the enzyme will denature, or become inactive due to a conformational change in shape (Campbell 100). Substances known as inhibitors can also stop an enzymatic reaction by either directly binding to the active site or by binding to the enzyme at a different site on the enzyme which changes the shape of the enzyme. In this experiment, NaOH was the inhibitor used to stop the enzymatic reactions. NaOH is very basic and when added to a solution, will cause a drastic increase in pH, causing denaturation of the enzyme. The amount of product formed could be calculated by placing the test tube in a spectrometer after the addition on NaOH. A spectrometer measures the absorbance of a solution, which helps compare how much of a substance is in a solution.
I hypothesized that the rate of the reaction would increase, producing more product as the amount of ACP in solution was increased because more enzymes allow for more substrate to be converted to product. The same hypothesis was made that when we increased the substrate, p-nitrophenyl phosphate, the amount of product produced would increase as well because there would be more substrate that could bind to the enzyme and be converted to product. For the environmental experiments, both temperature and pH, I predicted that the amount of product formed would increase with the temperature and pH, but then begin to decline after the enzymes reached optimal conditions. In other words, at the optimal temperature and pH, the enzyme velocity would be greatest, producing the most p-nitrophenol. Also, I predicted when the pH and temperature became too extreme, the enzyme would no longer be reactive due to denaturation. Overall, enzymes are very specific proteins that play a key role in metabolic processes and like all other proteins have optimal conditions under which they function most successfully.
Materials and Methods:
For a complete list of the materials and methods used in this lab please reference the laboratory manual (Lombard and Terry 92-103).
As seen in figure 1, as the amount of p-nitrophenol increases, the absorbance of the solution increases as well. The amount of p-nitrophenol that gives the greatest absorbance of 2.250, is .375micromoles. Oppositely, with no p-nitrophenol, the absorbance is 0.
Figure 1
Figure 2 shows a general increasing trend in production of p-nitrophenol produced as the amount of enzyme, ACP was increased. The amount of p-nitrophenol was greatest when the amount of ACP in solution was greatest, 1.00milliliters. Oppositely, with 0.00milliliters of ACP, there was no production of p-nitrophenol.
Figure 2
Figure 3 shows the effect of substrate concentration on the production of a product. Similarly to figure 2, the graph shows an increasing trend in product production with the amount of substrate, p-nitrophenyl phosphate. The amount of p-nitrophenol produced was seven times greater when there was 1.00milliliters of substrate compared to when there was 0.0millilters.
Figure 3
Figure 4 shows an increasing amount of product formed as pH increases, but then begins to decline after a certain pH. The amount of p-nitrophenol produced was the least, .003micromoles, at a pH of 9 and greatest, .138, at a pH of 5. After a pH of 5, the amount began to decrease. Before a pH of 5, the amount increased.
Figure 4
Figure 5 shows the same general trends as figure 4. As the temperature is increased, the amount of product increases and then begins to decline after a certain temperature. The temperature that formed the greatest amount of p-nitrophenol was 50 degrees Celsius, producing .40micromoles. The temperature that produced the lowest amount was 100 degrees Celsius, giving only .004micromoles.
Figure 5
The overall results of the experiment showed the correct general trends, in regards to the effects of environmental and chemical factors on ACP. As expected, the absorbance of the solution increased as the amount of p-nitrophenol was increased. This makes sense because what the spectrometer is reading is the amount of p-nitrophenol ( the yellow color of the solutions). So therefore, is there is more p-nitrophenol added to the solution, there will be a greater absorbance.
Changing the enzyme concentration affects the amount of product formed, as seen in Graph 2, and Table 2. Previously it was hypothesized that as the amount of enzyme was increased, the amount of product formed would increase as well, and the results fully support this. With only .05 milliliters of ACP present, the amount of p-nitrophenol produced was only .04micromoles. Oppositely, the solution with 1.00 milliliters of ACP produced .357 micromoles, almost nine times as much. This makes complete sense, because with more enzyme in the solution, that means more active sites were available for the binding of substrates, allowing for more product to be produced. In contrast, if the amount of enzyme was decreased, the opposite would be expected to occur since there would be less active sites available. Similarly, increasing the amount of substrate will also increase the rate of the reaction, because “the more substrate molecules available, the more frequently they access the active sites of the enzyme molecules. (Campbell 99)” As seen in Graph 3, Table 3, values went from .002micromoles of p-nitrophenol to .128micromoles of product as the amount of substrate, p-nitrophenyl phosphate, was
increased from 0.0ml and 1.0ml. The results fully confirmed my hypothesis that an increase in substrate would produce an increase in product.
As stated earlier, every enzyme has an optimal pH value at which it works the best. Looking at Graph 4 and Table 4 the results for the pH experiment supported my hypothesis that the amount of p-nitrophenol produced would increase with the pH until it reached the optimal pH. It would then begin to decline as the pH value continued to increase and migrated away from the optimal pH. From the results, one can see that ACP worked best when placed in a solution with a pH of 5, this being the enzymes optimal pH value. When placed in solutions with pHs of 3 and 9, the amount of p-nitrophenol produced was lower than when placed in solutions with pHs of 4 and 7. This is due to the fact these pHs are closer to the optimal pH than the other two. This makes sense because the further away the pH is from optimal conditions, the reactivity of the ACP will decline, inhibiting the production of p-nitrophenol. That is why the solution with a pH of 4, the closest pH to optimal conditions produced .054 micromoles of p-nitrophenol and the solution with the pH of 9, the farthest away from optimal conditions, produced only .003 micromoles of p-nitrophenol.
The same concept applies for the experiment involving different temperature. As with pH, every enzyme has an optimal temperature. Both Graph 5 and Table 5 favored my hypothesis that the enzyme would work the best at an optimal temperature, but as the temperature moved away from optimal conditions, both increasingly and decreasingly, the enzyme activity would decrease causing the amount of p-nitrophenol to decrease. Looking at figure 4, one can see that the ideal temperature for ACP was 50 degrees Celsius because the amount of p-nitrophenol produced was .4umoles, almost three times greater than any of the other temperatures. This is because at the optimal temperature, the substrates collide with the active sites of the enzymes more often, causing more product to be produced (Campbell 100). The velocity of the reaction is at its maximum. At 100 degrees Celsius, almost no p-nitrophenol was produced. This is due to the fact that as the temperature continues to increase past the optimal, the hydrogen bonds that stabilize the active shape of the enzymes break, causing the enzyme to convert to an inactive shape. This is known as denaturation (Campbell 100). This can further be explained by the extreme specificity of the enzyme.
Although the results supported my hypothesis about the general trends of the experiments, the actual data was not exactly what was expected. As with any experiment, there was a number of human errors that could have contributed to the faulty data. The pippetors that were used were not exactly the best measuring devices. It was hard to get the exact amounts of liquids such as volume of ACP and its substrate p-nitrophenyl phosphate. This would have effected the reaction and the amount of product formed. Also, every time a test tube was placed in the spectrometer, we did not remember to wipe it with a Kim wipe before placing it in. This along with the fact that the spectrometers could have become unbalanced after using the blank tube, would have given faulty absorbance readings. These readings when examined with the standard curve, would led us to believe there was more or less product produced, than the actual amount. However, the biggest contributor to error was the addition of NaOH. When this was added to the solution, the reactions in the test tube stopped, so therefore no more product could be formed. We were supposed to add NaOH exactly five minutes after the reaction started. In most cases we either added it too early or too late. If it was added too late, the amount of p-nitrophenol produced would be greater since the reaction was given more time to occur. Oppositely, if added too early, the amount of product would be less than expected since the reaction was not given enough time to proceed. There was a general trend in the faulty data readings. The absorbance readings for test tube 5, were always further away from the expected values than test tube 1. This is because the NaOH was not added to each tube at a time, but in sequential order with the test tube numbers. This allowed the reaction in test tube 5 to proceed longer than in test tube 1, allowing more product to be produced, giving a higher absorbance reading than expected. In fact, this trend was shown in all the test tubes. In increasing order of test tube numbers, every absorbance was more off than expected.
I would change a few things about this lab. Firstly, I would have used a micropipette instead of the ones that we used because they would give more precise measurements. Also, I would have had five people in each group so that everyone could add NaOH to the solutions at the same time, stopping the reactions simultaneously.

Enzyme Deficiency

Summary:   A short overview of enzyme deficiency, a serious disorder caused by a genetic defect. Enzyme deficiency can lead to many kinds of diseases, and at present only one sure cure has been developed.

Enzyme deficiency is caused by a genetic defect in the debrancher enzyme. It greatly affects the breakdown of glucose in the body. The disease is a recessive trait that must be present in both parents for it to affect the child. For most people the symptoms can include loss of mental and physical functions, and a premature death. For these reasons, the disease is taken very seriously.

There are many kinds of diseases related to Enzyme deficiency including Aspartylglucosaminuria, Fucosidosis, and Galactosialidosis. Each of these is a different kind of enzyme that is missing in the person’s body. Although, they are not truly different diseases, they are smaller parts of the Glycoprotein Disease. The disease happens in the Lysosome of a Cell. Sugars are constantly being broken down and reused. In people with Enzyme deficiency there is a genetic defect which prevents sugars from being broken down. This will cause sugar to build up, and can cause severe heal issues.
Currently the only sure has come out of the lab of Doctor Stephen Barrett. His drug is called Nu-Zymes. This drug is supposed to add the enzymes that the body is missing. Nu-Zymes does this by breaking down fats in sugars in the body taking the job of the Lysosome in the body. This drug could help thousands of people with there enzyme deficiency problem.

Enzyme Activity

Summary:   Experiment Aim: To determine the effects of substrate concentration variation on the activity of the enzyme pepsin. Also to determine the level of substrate concentration at which the enzyme pepsin functions most efficiently.

Experiment Two – Substrate Concentration
AIM: To determine the effects of substrate concentration variation on the activity of the enzyme pepsin. Also to determine the level of substrate concentration at which the enzyme pepsin functions most efficiently.

HYPOTHESIS: The percent of substrate concentration that the enzyme pepsin will function at its optimum will be 10%.INDEPENDENT VARIABLE: The concentration of the substrate (egg albumin) used in the experiment.DEPENDENT VARIABLE: The efficiency of the enzyme in acting and breaking down the protein in the egg albumin, i.e. how much egg albumin is dissolved.CONTROL: The HCl solution without the enzyme pepsin.EQUIPMENT:☺46 large test tubes☺1 beaker☺2 thermometers☺ Pepsin powder (2g)☺ Distilled water☺ Hydrochloric acid (HCl-1 molar)☺ Egg albumin☺ Test tube rack x4☺ Data Logger + Light Probes

☺ Transformer
☺ Computer + Tainlab
☺ Light Globe
☺ Pipette
☺ Syringe
☺ Black Box Set-up (See Diagram 1)
☺ Bunsen
☺ Test tube holder
☺ Matches
☺ Retort stand
☺ Filter funnel
☺ Muslin
1.Both the pepsin and egg albumin solutions were prepared.
a) Pepsin solution- 10ml of HCl were added to 100ml of distilled water. This solution was halved and separated into two separate beakers. 2g Pepsin powder was added to one beaker and this beaker was labeled Pepsin/HCl solution. The other beaker containing only the HCl solution was labeled HCl solution.
b) Egg Albumin –
☺Pure albumin- 30ml of pure albumen was heated until the solution became opaque.
☺90% Albumin solution- 27ml of albumen were added to 3ml of distilled water and the solution was heated until it became opaque.
☺80% Albumin solution- 24ml of albumen were added to 6ml of distilled water and the solution was heated until it became opaque.
☺70% Albumin solution- 21ml of albumen were added to 9ml of distilled water and the solution was heated until it became opaque.
☺60% Albumin solution- 18ml of albumen were added to 12ml of distilled water and the solution was heated until it became opaque.
☺50% Albumin solution- 15ml of albumen were added to 15ml of distilled water and the solution was heated until it became opaque.
☺40% Albumin solution- 12ml of albumen were added to 18ml of distilled water and the solution was heated until it became opaque.
☺30% Albumin solution- 9ml of albumen were added to 21ml of distilled water and the solution was heated until it became opaque.
☺20% Albumin solution- 6ml of albumen were added to 24ml of distilled water and the solution was heated until it became opaque.
☺10% Albumin solution- 3ml of albumen were added to 27ml of distilled water and the solution was heated until it became opaque.
J 0% Albumin solution- 30ml of distilled water.
  1. The data logger and light probe apparatus were set up at one end of the black box. A light globe, attached to a transformer, was set up at the opposite end, but left switched off. (See Diagram 1) The data logger was set-up to take readings ten times per second for sixty seconds. The transformer was set on “D.”
  2. 5ml of Pepsin/HCl solution were added to half of the test tubes. These were placed in a test tube rack and labeled.
  3. 5ml of HCl solution were added to another twelve of the test tubes. These were placed in a second test tube rack and labeled.
  4. 3 drops of Universal indicator were added to one test tube of Pepsin/HCl solution and to one test tube of the HCl solution and the pH was measured to ensure it was 2.5-3.5. The pH for each was recorded. These test tubes were then set aside from the others.
  5. 5ml of each Albumin solution, from 100% to 0% were added to two test tubes.(Total of 22 test tubes). These were placed in a third and fourth test tube rack and labeled with the corresponding percentages.
  6. One beaker was filled with 200ml water.
  7. One test tube containing HCl solution and the test tube containing 100% Albumin solution were placed into the beaker.
  8. One thermometer was placed inside each test tube in the beaker. The beaker was then heated in a water bath until the two solutions reached a desired temperature of 36.4°C.
  9. The test tube containing 100% Albumin was placed into the black box via the opening in the lid and the HCl solution was poured into the 100% Albumin. The light globe was turned on. The light probe was then activated, and the amount of light allowed to filter through the solution was measured using the light probe ten times a second for sixty seconds using the data logger.
  10. The graph, plotted by the data logger, was saved, and the light probe was then stopped and data logger reset. The test tube was removed from the black box, its contents disposed of, and the light globe turned off.
  11. Steps 8-11 were repeated, but the test tube containing HCl solution in Step 9 was replaced with the test tube containing Pepsin/HCl solution and then heated to a desired temperature of 36.4°C before being tested.
  12. Steps 8-12 were repeated. The solutions in Step 8 and 12 were replaced with the 90% Albumen solution.
  13. Steps 8-12 were repeated. The solutions in Step 8 and 12 were replaced with the 80% Albumen solution.
  14. Steps 8-12 were repeated. The solutions in Step 8 and 12 were replaced with the 70% Albumen solution.
  15. Steps 8-12 were repeated. The solutions in Step 8 and 12 were replaced with the 60% Albumen solution.
  16. Steps 8-12 were repeated. The solutions in Step 8 and 12 were replaced with the 50% Albumen solution.
  17. Steps 8-12 were repeated. The solutions in Step 8 and 12 were replaced with the 40% Albumen solution.
  18. Steps 8-12 were repeated. The solutions in Step 8 and 12 were replaced with the 30% Albumen solution.
  19. Steps 8-12 were repeated. The solutions in Step 8 and 12 were replaced with the 20% Albumen solution.
  20. Steps 8-12 were repeated. The solutions in Step 8 and 12 were replaced with the 10% Albumen solution.
  21. Steps 8-12 were repeated. The solutions in Step 8 and 12 were replaced with the 0% Albumen solution.


Because it was not possible to test every sample at precisely the same time, error may have occurred due to variation in environmental temperature. Whilst each test was cooled/heated to the desired temperature, the surrounding environmental temperature would have had an effect on the cooling rate on the test tube containing the Albumin/HCl or Albumin/Pepsin solutions. However this would not have had a significant effect on the results because the experiment was conducted over a relatively short period of time, in which the temperature did not vary greatly.
The absence of a Colorimeter led to the use of the Black Box apparatus to measure the amount of light transparency through the solution. While precautions were taken to ensure that this apparatus would take readings accurately, some errors may still have occurred. The box was painted black in order to absorb light rather than reflect it, which would have made the light probe readings inaccurate. A tunnel was set up to ensure that the light from the globe was directed directly through the test tube rather than spread throughout the box. Although these precautions were taken, there was still a fairly high margin for error. However these errors are difficult to avoid whilst using an apparatus such as the one used in the experiment. To obtain more accurate results, a Colorimeter could be used. However in this instance this equipment was not available for use.
One significant error did occur whilst conducting the experiment. When testing the pepsin on the 70% albumin solution, there was a data logging malfunction which led to the results only being logged for thirty seconds of the experiment. In order to correct this malfunction, the test would need to be repeated. Due to time restrictions this was not possible. An incorrect graph in this case may have led to an incorrect average light transparency, which would therefore impact, on the results showing average light transparency in comparison to substrate concentration.
Another source of error was through computer and data logging. While this apparatus is fairly accurate, it is possible that some errors may have occurred. The light probe readings may have been affected by sources of light other than the light globe. As mentioned, the only way to ensure that this did not happen would be to use a Colorimeter.
An advantage of using the Black Box/Data Logger apparatus was that, instead of a single reading as given by the Colorimeter which would have to be recorded and graphed manually, the data logger gave an accurate graph.
Another error, also associated with the Black Box/Data Logger apparatus was the placement and fixture of the test tube whilst the light probe readings were being logged.
It was important to have each test tube fixed in exactly the same position to ensure that the light transparency readings were not affected by the distance of the test tube from the light probe and light globe.
If these were not kept constant it greatly affected the readings on the graphs from one test to another. Whilst the test tubes were placed so that they were on level with both the light probe and light globe, and were fairly firmly fixed in the same position, there was still a margin for difference, and therefore a margin for error. To further unsure that these errors did not occur, a more fixture that did not allow movement of the test tube could be used.
One of the main sources of error in this experiment occurred due to the solidification of the high percentage albumin solutions. At high concentrations of albumin, when heated, the albumin solutions solidified. While the pepsin solution did still work to break down the substrate in some cases, it was found that “clumps” of albumin remained floating in the solution. Because of the use of sensitive data logging equipment this led to a high level of error. The light probe takes an accurate reading through only a small section of the test tube. If in this small section lay solidified albumin, then readings may be taken that would not reflect the results of the experiment. This led to many errors in the experiment, and was unavoidable when using high concentrations of albumin. However as the concentration decreased, and the solution no longer solidified when heated, this error was not present. This error did mean that the results gained in the experiment were not reliable or valid because it was an unfair test. In order to make the experiment valid, the amount of light transparency through the test tube and contents should be constant throughout. This was not possible to maintain when using high concentrations of albumin, which solidifies.
Originally, 1ml of albumin solution was to be used in each test. When tested, it could be seen that this was insufficient when trying to determine the effect of 5ml of pepsin solution on the albumin. The amount of albumin solution in each test was increased from 1ml to 5ml.
From the results of the experiment it can be seen that it was not a valid one. The results show no trends or patterns similar the results predicted, except with the exclusion of the 50%, 60%, and 70% tests. It can be deduced that possible errors in these tests led to inaccuracies in graphing which did not allow the expected trends to emerge in the results. However, when the averages of these tests were excluded, a pattern similar to that predicted can be observed. That is, with the decrease in substrate concentration came an increase in light transparency. While this pattern can be seen, due to the necessary inclusion of all tests in the results, it is found that the results obtained are not valid.
While the experiment did address the hypothesis in a real way, the high margin for error meant that any results obtained were not a fair representation of the effect of substrate concentration on the activity of the enzyme pepsin.
When observing the results, it must be taken into consideration that whilst the 100% solution was pure egg white, it was not pure albumin. The actual percentage of albumin in the white of a hen’s egg is 58.9 %. Therefore, when analysing results this must be taken into consideration.
Whilst conducting the experiment, there were several safety precautions that were observed to ensure the safety of the experimenter. Whilst handling and measuring chemicals such as HCl care must be taken to ensure that spills do not occur. All beakers, flasks, and other glass equipment must be kept a safe distance from the edge of benches, and handled with care. When heating using a Bunsen burner, it was ensured that the Bunsen was kept at a safe distance from the edge of the bench, and a test tube holder was used to heat the contents to avoid burns. Safety goggles were worn to prevent eye damage in the case of spills. Care was taken when adding the contents of the Albumin/Pepsin and Albumin/HCl test tubes to ensure that spills did not occur which would lower the accuracy of the results obtained.
The results of the error were found to be invalid due to error by both the technological equipment used and unavoidable substrate concentration error. However, the predicted results through preliminary research, that is that with the decrease in substrate concentration came an increase in light transparency, can be explained.

Ecosystem Lab

Summary:   Provides the details of a biology lab which attempts to create an ecosystem that could maintain it self forever without outside interferences. Describes a terrestrial ecosystem which was formed in a bottle that was sealed virtually airtight. Details the success of the hypothesis and what mistakes were made.

Introduction: In Biology we each attempted in groups to create are own ecosystem that could maintain it self forever without outside interferences. We had the choice of a terrestrial ecosystem or an aquatic one, in my group we choose terrestrial. Our terrestrial ecosystem was formed in a bottle that was sealed virtually airtight. We were hoping the ecosystem could maintain it self if we put enough plant life in it to create enough oxygen for the organisms and if we put enough water in to support all the life forms. The water was supposed to condense into the atmosphere of the bottle and then release when it couldn’t support anymore.
Materials: 2 Leiter plastic bottle, water, moss, 1 cricket, 1 inch of soil, 1 block of grass, 1 red worm, 2 meal worms, meal for the meal worms, gravel, thermometer, and pH paper
Procedure: The first thing we did was collect our materials and begin to cut the bottle, we cut about the top third off. After removing the top we placed the gravel in then the soil, red worm, grass and moss, cricket, and mealworms. We then proceeded to take both the temperature and pH level in the bottle before sealing it. The bottle was then sealed and put on the windowsill from 9/25 through 10/4 for observation and documentation. Once we had our observations, data, and conclusion and we took our final measurements we then disposed of the bottle and its contents.Data:Conclusion: In the ecosystem we created we began with a cricket, red worm and two mealworms we were left with dead bodies and moldy food. As you can see we did not create a self-sustaining ecosystem. The reasons for this is that we put the bottle in intense sunlight for to long, did not include enough water/food and we did not plant the plants deep enough to complete their tasks. Unfortunately this experiment disproved our hypothesis and denied us the chance to witness an ecosystem grow and evolve. On the plus side I believe we learned much for through failure then we would have if we had succeeded because this showed not only what was wrong about how we created the ecosystem but why it was wrong. In addition through our mistakes we were able to create limiting and necessary factors to create a correct ecosystem.

Mount St. Helens

Volcanoes have been around since the beginning of time, they’re very powerful and dangerous. These natural disasters can kill thousands of people, animals, and plant life in a matter of seconds. This essay will explain the history, the effects on both cultural and natural environment, and effects on humans of the most famous volcanic eruption in Washington State of Mount St. Helens.
Mount St. Helens is a Stratovolcano. Stratovolcanoes are formed by the gathering of lava and tephra and they’re associated with convergent plate boundaries. The oldest rocks at Mt. St. Helens are about 40,000 to 50,000 years old. It began erupting about 2,500 years ago. It erupted several times during the 19th century, a major eruption in 1843. on the 20th march, 1980 a large group of earthquakes began to shake; and on the 25th of march 1980, the first steam explosion began. Before the eruption, the area around the mountain was rich with tourism for its natural beauty. The Spirit Lake at the bottom of the mountain was blanketed with ancient forests with 800 year-old-trees. After the eruption of the 1980, the trees were knocked over or snapped in half and were left standing dead. The most naturally beautiful place was ended in a deserted landform.

The eruption of Mt. St. Helens has changed the face of the land. It changed the landscapes in some ways. Many animals and plants fall victims of this unsightliness eruption. The explode of Mt. St.. Helens had a force equivalent to more than 27,000 atom bombs. In few hours of the eruption, 234 square miles of forest lands were destroyed, and almost all life on the mountain disappeared. After the settlement of the ash, the area appeared in a desolate, uninhabitable wasteland. The mountain released gases to the atmosphere, which was one of the century’s bigger eruptions. Also, during the eruption a sudden collapse of the volcano’s north side released the huge pressure that has been building inside the mountain. The force of the explosion and its temperatures which reached 600 degrees F, stripped trees from hillsides as far away as 6 miles from the volcano. Trees were killed by the strong heat of the explosion, in which they were left standing but dead. This area is known as the Standing Dead Zone
Around the area of Mt. St. Helens, the plants and animals were almost completely wiped out. It is estimated that 5,000 blacks- tailed dear, 1,500 Roosevelt elk, 200 black bears, and 15 mountain goats fell victims. Millions of fish, birds and insects were also in the way of the eruption. Geologists say that it’ll take centuries to re-grow an ancient forest of trees.
The cost of 1980 eruption was estimated $860 million dollars. More than 200 homes along the south and north sides of the river were either washed away buried or otherwise damaged. On eastern Washington highways, the ash blocked the air filters of car and truck engines, leaving 5,000 owners alone and helpless. Two days after the eruption; more than half of he vehicles operate by police and emergency services were out of service. The roads were blocked enough to drive and many highways were damaged.
People build a small town at the bottom of Mt St. Helens at the east direction because it was a beautiful place to live. Mostly, those people who lived near, they worked there, in the woods. The eruption was very destructive and had an immense physical as well as emotional loss, in which the jobs in the forests such as logging were stopped. There was 27 bodies never found and 7 people were killed by a plane crush, a traffic accident and ash fall, with more others of a total of more than 60 people lost their lives directly by the eruption. More than 1.00 people were rushing to escape the explosion. At Washington State University in Pullman, 3,358 students dropped out before the end of the term, to avoid lung diseases such as lung ailment.
Mount St. Helens eruption was powerful and destructive natural disaster, which killed many people, animals and plants. It has been building for thousands of years and suddenly erupted where it let the most naturally beautiful place to end in a deserted landform, uninhabitable wasteland. Volcanoes are powerful and dangerous to live near them. They can destroy thousands of square kilometers in seconds, which is really destructive.