Dissections

Starfish Dissection:

Our species of starfish was an Ophiuroidea, which are brittle stars and basket stars. We begin by placing the starfish with it's aboral surface, which is covered with spines, facing upward. Start cutting into one of the arms of the starfish and then peel back the surface to reveal the pyloric caeca and, below that, the tube feet. The bulb like tops on the tube feet are called ampulla. In the center of the starfish is its madreporite, which is on top of the central disk and is where water enters into through and to the water vascular system. 

Grasshopper Dissection

Since it's easier to see the important internal organs and nerves, we had the grasshopper's dorsal side facing us. Taking a pair of scissors, we began cutting at the bottom in an upward motion. We were sure to cut as slow and close to the exoskeleton as possible so not to cut any of the ventral nerve cord. In order to see the brain and dorsal ganglion, we could've continued cutting higher into the head. Once we get to the top near the neck region, we started cutting toward the sides. We did this by cutting from both the top and bottom portion of the prothorax. By spreading the exoskeleton to the sides, we revealed the inside of our grasshopper. We also inspected many of the outer parts such as the tympanic membranes which they use for hearing and the antennas which they use for feeling surfaces and sensing danger around them.  

Perch Fish Dissection:

Turn the perch onto its dorsal side and begin a rectangle shaped incision in the operculum and peel back in order to reveal the organs. Below the operculum are the bony gill rakers. In the gills are the cartilage support called the gill arch along with soft gill filaments that make up each gill. At the posterior end of the stomach are the coiled intestines. The pericardial cavity contains the heart. The upper part of the body below the lateral line is the swim bladder.

Crayfish Dissection:

First step is to lay the crayfish on its side. Locate the cephalothorax and the abdomen region. Turn it with its dorsal side upward and locate the rostrum (beneath it should be the eyes). Locate where the appendages in the head region are and find the antennae. The, study the mouth which have mandibles behind the antennae. The largest part of the appendages is the chelipeds or the claws. Behind each of these are walking legs. Then turn the crayfish central side up to locate the appendages from the ventral side. Lift away the carapace and using scissors cut the case of the tail and lift the parts of the carapace to reveal the gills and other organs. The maxillae passes the food and travels down the esophagus to the stomach. When opened up, one is able to see the intestine, the stomach and the anus of the crayfish.In the tail, we can see the intestines and tail muscles which help crayfish swim through the water.

Electrophoresis Lab

Purpose: The purpose of this lab is to analyze unknown DNA to determine the number of cut sites for each restriction enzyme and the positions of those cut sites relative to one another. The goal was to use electrophoresis to help us visualize the placement of each of the bands compared to one of the master bands in order to find out the size of each.  

Introduction: Restriction mapping is a critical step in analyzing and characterizing a new DNA sequence. A restriction map of a piece of DNA can be compared to a fingerprint, something to identify each piece. In order to set up this lab, we were to use three restriction enzymes, PstI, HpaI, and SspI. The purpose of this lab, as stated before, is to find out the number of cut sites present in the DNA sequence for each restriction enzyme and the positions of those cut sites relative to one another. In order to do this, the DNA should be loaded into each well of the gel and analyzed after gel electrophoresis has taken place. 

Methods: Fortunately, the agarose gel was already pre-made when we did our experiment, so we did not have to worry about casting the agarose gel. Our first task was to simply load the DNA into the gel. We began by drawing samples into the pipet, making sure we expelled any excess air so that air bubbles wouldn’t form in the wells. We steadied the pipet over the gel and dipped the pipet through the surface of the buffer, positioning it over the well, and letting out the liquid. We did this a total of 4 times, one for the comparison or control group, and the rest for each of the three different restriction enzymes. The next task was the actual electrophoresing process. This consisted of an electrophoresis chamber which was connected to a power supply with high voltage. Our teacher monitored the electrophoresis and took it out when he saw fit and then we loaded it onto the staining tray. After being stained, we were given back our trays to be able to examine the movement of each restriction enzyme bands through a lightbox. The lightbox helped see the bands better so that we could label them and compare by size marker. 

Discussion: The movement of the different bands in each well were dependent on their varying sizes. The well that showed the farthest movement down the gel towards its positive end was well Pst I. This can lead us to assume that the DNA strands that were present in that solution had strands that were cut thin enough so as to be able to make its way so far down it's given well. In contrast to that, the well of Pst I also had a marker in it that did not travel far in comparison to the rest, meaning that it's DNA strands were much too large to move much distance at all. When compared to the constant well that was the Marker well, most other wells only conducted of a given 2-3 bands. This would lead us to assume that the DNA we were working the wells with we're relatively basic in the sense that not many bands were present or shown. ThBeing pre-given approximations for the positions where each marker should have ended, accuracies in their placement verified that the correct loading substance was placed into its appropriate well. Furthermore, after constructing the positions of the various recorded bands into a visual circular chart for every well and it's bands, the lengths in which they were recorded straight on the gel came to match with the circular graphs, 

Data:

Conclusion: Through the use of gel electrophoresis, we were able to identify where certain cuts in all restriction enzymes occurred. We were able to label the bands we saw under the lightbox and compared it with the control well in order to find out our efficiency. After taking a close look, we realized not all of the bands that were supposed to be present were visible. This may have been due to an error in loading the wells. We realized after the put away our try to the electrophoresis station that one of our tubes had not been fully pipetted into the well and that may have caused some inaccuracies in our results. We acknowledged our mistakes and realized it could have been avoided by making sure we expelled all excess air from out pipet. However, aside from small mistakes, our data was pretty accurate in reflecting what should have been seen according to our data. Wells 2-4 were all supposed to have the same total size of DNA fragments and as seen in our data, it was within the same range, since it was an estimate of course. As different fragments of DNA moved at different rates and therefore different positions, we used this data to construct diagrams of said fragments.  

pGlo Lab

Purpose: The purpose of this experiment was to oversee the process of genetic transformation. We were trying to see how this procedure accounts for the pGlo plasmid's ability to code for Green Flourescent Protein (GFP)

Introduction: In this lab we were to perform a procedure known as genetic transformation. This protein gives the organism a particular trait. This involves the insertion of a gene into an organism in order to change the organisms trai. We used that procedure to transform becateria with a gene that codes for GFP. The source of this particular gene is from the bioluminescent Jellyfish Aequorea Victoria, which causes them to glow in the dark. Once the procedure is completed, the acquired jellyfish gene will cause the bacteria to glow a green color under ultraviolet light. In this experiment, we were to learn about the process of moving genes from one organism to another with the help of a plasmid. A plasmis contains genes for one or more traits needed for its survival. Transferring of said plasmid occurs between bacteria to allow them to share these beneficial genes and hence, the bacteria adapts to its new environment. In this experiment, the occurrence of bacterial resistance to antibiotics is due to the transmission of plasmids. The pGlo plasmid encodes the gene for GFP and the gene for resistance to the anitiotic ampicillin. The gene for GFP can be switched on in transformed cells by adding the sugar arabinose to the cells nutrient medium. Transformed cells will appear white  without the sugar, and glow green with the arabinose. 

Methods: At the start of the lab, we labeled 4 tubes with either +PGlo, -PGlo, (control group), transformation solution, and broth. Then we pipettes some transformation solution to both the negative and positive tubes and then, we put them in ice. After that, we scooped bacteria out of a Petrie dish and spread the E. Coli in both with a sterile loop and mixed well.  However, we put plasmid only in the positive pGlo container.  In order to compare results, we labeled 4 different Petrie dishes. After, we put the tubes back in ice for 10 minutes and then we used heat shock by putting it in water (45 degrees Celsius) for 50 seconds and back in ice for 2 minutes. Using a pipette, we put broth in both tubes. Using a pipette, we put pGlo according to how the Petrie dishes were labeled as such. Then, we spread out the solution with a loop to increase surface area. The last step was to put it in an incubator at 37 degrees Celsius for 1 day. He next day, we took it out and using a UV flashlight, we measured growth in Petrie dish and it's ability to glow under the light. 

Data:

Discussion: After taking it out of the incubator, we were to analyze the growth and ability of the E. Coli bacteria to glow under UV light. We had the most growth with -pGlo LB, no growth in -pGlo LB/AMP, and some growth in both +pGlo/AMP and +pGlo/LB/AMP/ARA. It was clear since before we did the lab that -pGlo LB/AMP would have no growth because all the bacteria cultures that would've grown would have been killed off by the AMP(Ampicillin) which is an antibiotic.  -pGlo LB Was used as a control group because the bacteria was allowed to spread without the plasmid. +pGlo/AMP and +pGlo/LB/AMP/ARA Both had growth because the bacteria was made resistant to the antibiotic and were allowed to spread. However, +pGlo/LB/AMP/ARA was made to resist the antibiotic and the arabinose activated the pGlo gene which causes it to glow under UV light. These results are valid because we discussed what each of the Petrie dishes should have looked like. We were shown expected results of the dishes and out data was compatible. The Petrie dishes showed that the ampicillin killed the E. Coli that did accept the pGlo gene and we proved that the arabinose help the pGlo gene activate after certain genes have accepted the pGlo gene. 

Conclusion: The final results of our pGlo lab yielded an effectively added Aequorea Victoria that is the bioluminescence gene found in jellyfish showed through in the Petri dish of +pGlo with LB broth, Ampecilin and Arabanose sugar. Our hypotheses proved correct because we expected the fourth Petri dish, which held every additive in it, to not only accept the pGlo gene but also to isolate it on the account that we added the Ampecilin to eliminate any remaining genes that had not accepted to bioluminescence gene. As our final results matched the expected results fairly similarly, we can conclude that the lab went relatively successful. For improvements, we could have attempted to cause greater colony growth on the Petri dishes as that would have shown more efficiency in our dishes.

Yeast Cellular Communication

Purpose: The purpose of this lab was to see how growth signifies that cell communication occurs within a population during each stage of their cycle. We were able to see this growth as the populations multiplied over time

Introduction: Yeast is a unicellular organism. The cell of the yeast break down sugar into ethanol during alcoholic fermentation. It also can undergoes asexual and sexual reproduction. During sexual reproduction, the yeast cell change from single haploid cell to a gamete (sex) cell due to a certain chemical signal. There are two types of yeast cell: a-type and alpha type. Each type of cell secrete a mating factor that bind to the receptor on the other cell type. A factor would attach to alpha-type cell receptor. Alpha factor would attach to the a-type cell receptor. When the mating factors is attach to each of the cell, the two cells begin to fuse together to form a pear-shape gamete cell called shmoos. The two cells then finally come into contact to form a single cell that contain gene from a and alpha cell. When the condition is right, the cell will begin to divide during mitosis. The process that the yeast go through can be found in other cell. Yeast cell mate with each other. This is how yeast cell communicate with each other. Cell can communicate with each other by sending signaling molecule to the other cell which response to a particular signal. The cell response can be anything like mating or creating a new protein. Before signaling molecule can send signal to the cell, the signaling molecule have to bind to a receptor on the cell plasma membrane. When a signaling molecule bind to a receptor, like G protein-coupled receptor, it activate the receptor. The receptor then bind to G protein to activate it. This cause the GTP to displace GDP. G protein then diffuse across the cell to bind to the enzyme, causing it to activate. The activated enzyme then send a cellular response. Signaling molecule is then disassociate from the receptor. G protein then disassociate from the enzyme. GTP then turn into GDP. The cell is then able to reuse the G protein. Cellular communication then occur time after time like a cycle to produce many responses that are important to the cell.

Methods:

In this lab, we used 3 types of subcultures: a-type, α-type, and mixed, which contained the a-type and the α-type. We transferred a small amount of each yeast type to the water in the culture tube. We used toothpicks to transfer a clump of yeast 1 mm wide into the designated test tube. After each transfer we used a new test tube for the yeast. When we finished putting the yeast in the test tubes, we put 5 drops in the yeast suspension in the plates. After that we used new swabs when we were spreading the yeast suspension over a small area of the agar. We then counted the yeast cells by putting them in slides and looked at them under a microscope.

The three agar jars we used (alpha, A type, and mixed)

Scrapping off some yeast! Ew!

Mixing the yeast to the sterilized water!

Adding the yeast to the trays

Putting it on the slides

The microscope we used to see the slides

What the yeast cells should look like

Yeast growth (alpha type)!

So many yeast populations (mixed)! 

More yeast (a type)!

Data: 

Graph: 

Discussion: As time progressed, we saw that there was an increase in yeast growth. The yeast in our early trials began as single haploid cells and as time went by we were able to see developing double haploid cells and even some single zygotes. This is an interaction directly caused by cellular communication. Since the viles were not stored in incubators, this experiment was done solely at room temperature. As we can see by our graphs and our labeled pictures, all the types were increasing, but the biggest increase in yeast population was seen by the mixed culture. The heightened growth of this specific culture is caused by more (and different types of) yeasts which were able to give off more signals that let the other yeasts know they were present. As a result of this more yeast was produced. Our data is valid because as more yeast communicate with each other it more likely that reproduction will take place. This supported our hypothesis (yeast will increase in number over time) due to the results of the data and 2 graph. We believe our data for the 30 minute section could've been improved because our methods were not consistent. We only added broth to act as a mound for the Petri sample on our the second and third day. Therefore, our experiment could've been more accurate if only we used the broth and maybe did more trials that were closer apart (although our time was limited and was a constraint).

Conclusion: The expected result of an increase in cell population solidifies the fact that communication within the cells in the mixed Petri dish showed a substantially greater increase than the individual a type or alpha type dishes and greater communication occurs when there are various cultures present to send and receive cell signaling. Results could have varied to a massive increase in cell population should the vials have been chosen to be put in an incubator, as cells grow more rapidly in hotter temperatures as opposed to regular room temperature. We had earlier anticipated that the mixed sample would have the greatest increase in population due to it having two different cultures of yeast cells which is exactly what was shown in our graphs. This massive population in the mixed culture was probably on account of both a and alpha type cultures being ble to pruduce a higher level of communication and budding amongst themselves.

Chromatography/Cellular Respiration Lab

Chromotagraphy

Purpose: The purpose of this lab is to see the separation of plant pigments using chromatography. We tested this to be able to calculate the Rf values. We also wanted to measure the separation of the colors which represented the different kind of chlorophyll which were present in the spinach leaf. 

Introduction: Chromatography is the technique of separating and identifying pigments that contain a mixture of molecules. Adhesion is when dissimilar molecules stick to each other. Cohesion is similar to adhesion in the sense that the same molecules stick to each other.  The higher the color, the more adhesive properties it has. Solvents goes up through capillary action through which it carries any substance dissolved in it. Present inside the spinach we tested were different types of chlorophyll that emerged when we submerged in the solvent.  Carotene protects it from ultra-violet rays. Chlorophyll A absorbs most energy from wavelengths of violet-blue and orange-red light. Chlorophyll B absorbs light energy and blue light. Xanthophylls are oxygenated carotenoids that are synthesized within the plastids.

Methods: In this lab, we took a 12 cm strip of filter paper and cut it to a point at the tip. We filled a graduated cylinder with 1 cm of solvent. We then had to cut a piece of the paper and mark a line 1.5 centimeters from the bottom. We took a portion of spinach and (using a coin) extracted spinach pigment by smearing it on the paper. The smeared spinach pigment was done above the 1.5 cm line making sure it was secured with a stopper. We then barley submerged the tip of the filter paper into the solvent, enough so that the point of the paper took in solvent but not enough so that the solvent wouldn't make contact with the smeared spinach pigment. We waited for half an hour and marked the location of the solvent front before it evaporated. We marked the bottom of each band measured the distance. 

Data:

Discussion: For the light green to the pale yellow pigment, there was a consistent rate of distance between each band. Band 1 came in at 45 cm, band 2 was a distance of 48 cm, band 3 was 63 cm, and band 4 was 65 cm. band 5 varied the most in distance, measuring almost equidistant to the combined distances of bands 1-4. Band 5 measured at 96 cm. Band 1 and 3 were identified as chlorophyll a. Band 2 was identified as chlorophyll b. Band 4 was identified as xanthrophyll and band 5 was carotene. There was reasoning for as to why the different colored bands  came in the order that they did. Because chlorophyll a and b and xanthophyll were located near the bottom of the filter paper, we can safely say that it's adhesive properties are weaker than the band of carotene that was located higher up the strip of paper. This means that chlorophyll a and b along with xanthophyll cannot grab onto other surfaces or substances as well as carotene. Xanthophyll specifically is also less soluble and is slowed down by hydrogen bonding to the paper strip. We can also infer that their cohesive properties that allow their similar molecules to stick to one another are likely also as weak as their poor cohesive abilities. The band measurements did come out to match the predicted results and band order than we'd initially assumed meaning that the experiment results were successfully accurate. The experimental procedure as a whole was mostly successful. 

Conclusion:This experiment tested the relationship of the distance moved by a pigment to the distance moved by the solvent which was referred to as Rf. We used this calculation to test our hypothesis which is supported by our data table. We found out that different pigments migrated at different rates due to cohesion  and adhesion ability. The ones that traveled higher up the paper had greater adhesion property (Chlorophyll A, B, and xanthrophyll). We could have improved the experiment by leaving the strip submerged longer so that we may see more bands appear and this would have given us more results to give added accuracy. Also, more trials could help us compare our results and make sure the trends are consistent. 

Cellular Respiration

Purpose: The purpose of this lab was to test to see if light and chloroplast are required for light reactions to occur. This allowed us to see the effects of light and light deprivation. 

Introduction: When light is absorbed by leaf pigments, electrons are boosted to a higher energy level. Then ATP is produced. For this to happen, there needs to be a reduction of NADP to NADPH. However, in this experiment, DPIP is used as a substitute for NADP (electron accepter). When light strikes the chloroplast, the electrons are excited and changes the DPIP from blue to colorless. Then, ATP and NADPH combine with CO2 into organic molecules (carbon fixation). 

Methods: While the spectrophotometer was warming up, we set up an incubation area with a water flask in front of a light and test tube rack. We were provided with 2 bottles: one with boiled and one with unboiled chloroplast which were kept in ice the whole time. Different additions of phosphate buffer and distilled water were added to each test tube. We also added DPIP to test tubes 2-5. We put cuvette 1 (the control group) into the spectrophotometer and calibrated the lab quest. This allowed us to have a comparison to the other cuvette. However, cuvette 2 was covered in foil to keep light out. We added 3 drops of chloroplast to test tubes1-4 and immediately took a transmittance reading from the spectrophotometer. Then we put them in the light behind the flask and recorded a new transmittance reading every 5 minutes for 20 minutes. Additionally, the second attempt at the experiment was meant to allow us to come up with a way to show a more steady increase in our graphical data instead of the spikes in data we had acquired in our first attempt. 

Data:

Attempt 1 Graph:

Attempt 2 Graph:

Discussion: Our control group for this experiment was our cuvette the that was unsoiled and exposed to light because this sample would be the only beaker that would record and show the normal light transmittance that a common chloroplast would have. (Cuvette 1 was used to calibrate our spectrophotometer, so it is not in our data table, meaning our data results would begin with cuvette 2). The trends we found in the second attempt were that cuvettes 1,2, and 4 increased in transmittance percentage as time went on and decreased in absorbance. However, cuvette 3 decreased in transmittance percentage as time went on and increased in absorbance. This shows that regardless of light transmittance increasing or decreasing, there was an inverse relation with the absorbance of light. One thing that we found inconsistent with the collected data was that cuvette 4, which contained no chloroplast at all, showed an increase then decrease in light transmittance and an increase then decrease in light absorbance. What is boggling about this is that, because this cuvette did not contain any chloroplast, there really shouldn't have been any absorbance or transmittance of any kind because there was no medium for it light to travel through. The first attempt was littered with errors. We calibrated correctly, but we added the chloroplast directly to the cuvettes instead of the test tubes. We also waited too long to put the cuvettes in front of the light causing a delayed reaction. All the cuvettes we're not put it together which didn't maximize the time they could've all spent behind the light. This limited time resulted in only being able to perform two trials whereas there should've been four. However, the one of the trials did not fulfill the required time. The second attempt was a lot more successful because we completed all four timed runs for the required 5 minutes each, added the chloroplast to the test tubes, and instead of adding the chloroplast directly into the four cuvettes, we added the chloroplast into the beaker so that the chloroplast would distill in with the other substances in its respectable beaker instead of possibly overpowering the solution before when the chloroplast was added directly into its cuvette. This proved successful because after we distilled the chloroplast into the beaker as opposed to adding straight to the cuvette, the graphical data increased steadily and did not spike. Our data did not support our hypothesis because cuvette 3 decreased then increased when it should've done the opposite. 

Conclusion: This experiment tested how chloroplasts in different situations absorb and transmits light.  By using the blank cuvette with water to calibrate the spectrophotometer, we were able to individually calculate the amount of transmittance in each cuvette. Since cuvette 2, unboiled and light (originally in test tube 3) acted as the control group, we were able to compare the others to that cuvette. By looking at our data tables, we were able to conclude that transmittance and absorbance acted as reciprocals to one another. As transmittance went up, absorbance went down and vice versa.  After attempt one, we realized we needed to decrease the amount of chloroplast used so the graph would not spike up.  As a result of this, in attempt two we put the chloroplast solution directly into the test tubes instead of the cuvettes. This made our results more accurate and helped prove our hypothesis.

Enzyme Catalyst Lab

Purpose:
The purpose of this lab to analyze how enzyme affects the conversion of hydrogen peroxide to water and oxygen gas. In other word, how does the enzyme affect the rate of hydrogen peroxide breaking down into water and oxygen. We wanted to test how much enzyme we need to really start affecting the solution to change. The independent variable was how much of the enzyme solution we put into the hydrogen peroxide solution. The dependent variable was how soon the hydrogen peroxide changed to pink/brown and how much enzyme is needed to do so.

Introduction:

This experiment is all about enzymes and how they react to different situations. So what exactly is an enzyme? An enzyme is a substance produced by a living organism that acts as a catalyst to bring about a specific biochemical reaction. A catalyst is something that affects the rate at which the chemical reaction takes place. In this experiment, we will deal with enzyme-catalyzed reactions which means that the substance to be acted upon, the substrate represented in an equation as S, binds to an active site of the enzyme, represented as E. One advantage of enzyme-catalyzed reactions is that it makes the reaction require less activation energy so that products (P) of the reaction form. This is expressed with the following equation:

E + S -> ES -> E + P

It is important to know that each enzyme is specific for a particular reaction because of the amino acid sequence, which has an effect on its structure. Active sites in an enzyme interact with the substrate so that any substrate that changes the shape or blocks the active site will have a completely different purpose/shape than it did before. How can this happen? Well, salt concentration, pH, temperature, and activations & Inhibitors are four ways that enzyme activity can be affected. Depending on the amount of salt concentration, the proteins in the enzyme will denature and in turn become inactive such as with low concentration. On the other hand, concentrations that are too high will cause blockage. Denaturing of proteins also applies to pH and temperature. When the pH & temperature is too high or too low, it causes enzymes to become inactive, since most enzymes perform optimally at about neutral pH and temperature. Lastly, activations and inhibitors regulate how fast the enzyme acts.

In this lab, the enzyme used was catalase. It takes part in some of the many oxidation reactions that occur in cells, but the primary reaction catalyzed by catalase is decomposing H2O2 to form water and oxygen as shown in the following equation:

2 H2O2 -> 2 H2O + O2 (GAS)

Without catalase, a reaction would still in fact occur, but at an obviously slower rate. 

Methods: 

We started out this experiment by putting 10 ml of H2O2  into 7 separate beakers. Each beaker was labeled with a number ranging from 10 to 360 seconds (depending on how much time we would have to swirl it). Then, we added 1 ml of the catalyst. Now we actually got to "mix" the H2O2 by slightly swirling it. We also set a timer to keep track of how long we needed to mix it. Once the timer hit zero, we quickly added 10 ml of H2SO4. Then we put it under the burette and added one drop at a time of the KMnO4. We waited until the the mixture turned permanently pink/brown . This allowed us to see how well the catalyst and enzymes work and how it varies depending on the amount if time it has been in the H2O2 mixture.

Data:

Graph:

Discussion:

For the lab we filled out a chart with our results. The charts explain how long it took our base line. The intial reading was what the tube was filled at before we used it and the final reading was what it was after the reading. We took the base line and added the enzyme and kept on stirring for 10, 30, 60, 90, 180, and 360 seconds. After the time is down we would check and check how much KMnO4 it takes for it to give it a pinkish color. Our results are valid because we compared our results with the class and our data is very close to other groups. In the graph the blue line shows the H2O2 used and the red line shows the KMnO4 consumed.The longer we waited on the H2O2 the more of it was being used in the chemical process and the longer we waited on the KMnO4, less of it was being released because all the enzymes in the chemical reaction are being used.

Initially, we anticipated that, with more time passing between our addition of catalase into our solution of H2O2, the quicker we would be able to see a presence of color indicating the efficiency of the reacting enzyme that was catalase. This proved to be correct as our data began to show a decrease of used catalase from our burette as we began mixing it with our beakers that had been swirled with catalase for a longer period of time.

For example, the beaker that we added and swirled catalase with for a period a six minutes only required .5 mL of KMnO4 to be added until a pink coloration was seen to indicate a reaction whereas our beaker that was swirled for a shortened period of only 10 seconds required a larger quantity of KMnO4 to be added, a difference of 3 mL to our six minute beaker's .5 mL, in order for a pink color hue was seen in the solution. This showed that the more time that catalase was given with the H2O2 solution, the quicker a visual reaction would occur with KMnO4.

Additionally, our collected data showed an inverse relationship with the amount of KMnO4 consumed versus the amount of H2O2 used. Our data showed that when looking at the amount of KMnO4 used (here we are going to describe the amounts in terms of first, the beakers that had a shorter period of time to mix with catalase on to those who had longer time) began high at 3 mL for our 10 second beaker and then dropped down to a smaller amount of .5 mL used, as seen with our 6 minute beaker. However, the amount of H2O2 that was used in our 10 second beaker, the one which had used 3 mL of KMnO4, only .5 mL of H2O2 was used. This inverse relationship between KMnO4 and H2O2 became more evident as we observed the dropping amount of KMnO4 used in regards to the raising amount of H2O2 used as we increased the the time given for catalase to react with our beakers. The 6 minute beaker of H2O2 ended up using .5 mL of KMnO4 to a higher 3 mL of H2O2 used. These two beakers were our extremes and more clearly showed the contrast in use of the two kinds of solutions used in this lab.

We have to acknowledge that for some of our beakers, the time we spent swirling in catalase might have differed by some few seconds or so by either some means of loss of time or distraction of some kind and that may have altered results. For future tests, we should keep close attention to the time spent swirling the catalase with our various beakers for that specified time the lab calls for.

Conclusion: 

Once all data was accumulated from the previous procedure, the results showed an inverse relationship with the amount of KMnO4 consumed and the amount of H2O2 used. As the time that passed increased, KMnO4 increased from its initial 3mL down to a final .5 mL whereas H2O2 decreased from its initial .5mL up to 3mL. This shows that the increased time spent adding H2O2 lowered the amount of substrate needed to catalyze a reaction when in use of KMnO4. The trials exemplified the very aspect of how a present enzyme of catalase sped up the reaction of our KMnO4 solution. As the time increased where our catalase was mixed in with our solution supported the anticipated result that the presence of color in the initial colorless solution would occur more quickly, which shows that less KMnO4 is need as the amount of H2O2 is used. Because the addition of KMnO4 was done by hand, the precise amount of minimal substance that could be added until a color change was seen could be off by a, minute but still present, amount.