Bio Lab Report Erica Patterson September 10‚2013 Intro to cellular and molecular Biology Lab Abstract: In the Biology Laboratory Manual by Darrell S. Vodopich and Randy Moore are results to a similar experiment. The studied the hypothesis of carbon dioxide production by yeast fed sugar is not significantly different than the carbon dioxide production by the yeast fed in protein. Their hypothesis is the one that has helped formulate ours. We also will be answering the same to questions “What
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themselves. ⋆ Their presence does not affect the end product. ⋆ They only need a small effort to change a large amount of substrate. ⋆ Enzymes are very specific and usually only speed up a single reaction. ⋆ Their rate of activity depends on the PH of the substance‚ the temperature of the substance and the concentration of both the substance and the enzyme. An enzyme fuses with its substrate and this makes an enzyme-substrate complex. Once this reaction has occurred‚ the complex will break
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constant k of curds were higher for the gels having larger pores‚ which can be inferred by the syneresis changes (Table 2 ) and microstructure changes (Fig. 3B) of rennet curds made from different pH and temperature. Similar results had been reported by Pierre-Anton et al. (2003). The results also showed that lower pH acid curds had larger pores and denser
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When Chemicals React! Mr. Bell’s honors level chemistry class conducted an experiment during their lab demonstrations‚ this consisted of elements such as phosphorus and calcium chloride in their experiment. This along with another hydrogen based sunstance produced‚ what looked like a pinkish-looking substance inside of their flasks that were at their lab stations. Sophmore Kelly Caudel said‚ “ I actualley enjoy doing the experiments in this class‚ because it gives us a chance to get away from
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were experimented. We analyzed the change in absorbencies over time for varying substrate concentrations. There were four experimental assays which contained 1% enzyme solution‚ substrate solution of 0%‚ 1%‚ 2%‚ and 3% concentrations‚ guaiacol‚ and pH 7 buffer. At 2% concentration there was a greater enzymatic activity and at 3% concentration enzymatic activity decreased. The results were supported of our hypothesis. INTRODUCTION Enzymes are proteins that catalyze chemical reactions and are one of
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Determination of Florfenicol in Catfish by UV-mediated High Performance Liquid Chromatography (HPLC) 1. Introduction 1.1 Description of the Analyte Florfenicol (C12H14Cl2FNO4S) is a derivative of thiamphenicol. Its structure is identical to that of chloramphenicol – a synthetically developed antibiotic for veterinary use‚ such as treating a wide range of bacterial infections (Hayes p. 7). It is commercially available as 50 percent of Aquaflor® premix‚ which has been approved for the control of bacteria
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Name: Nikia Martinez Class: Biology 240L L3-1201 Assignment: Electrocardiography Lab Report Due: April 3rd 2012 Professor: Dr. B. Schoffstall Introduction In a normal human being the heart correctly functions by the blood first entering through the right atrium from the superior and inferior vena cava. This blood flow continues through the right atrioventricular valve into the right ventricle. The right ventricle contracts forcing the pulmonary valve to open leading blood flow through the pulmonary
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the percent yield by dividing the expected yield‚ the amount of product that should be produced based on your stoichiometric calculations‚ by the actual yield‚ the amount of product that is experimentally obtained from a chemical reaction. In this lab‚ I have determined the reaction for mixing two reactants together; I measured out 0.005 moles of each reactant‚ lead (II) nitrate and potassium chromate. I dissolved‚ mixed‚ and made them react to make products; I compared the mass of the two reactants
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Engine Lab Report Diesel Engine Load/N |Fuel Time/s |dH/mmH2O |Speed/r.p.m |Temp/℃ |Air consumption/kg/H |Fuel consumption/kg/H |Air-fuel ratio |Power/kw |Efficiency/ % | |40 |121.6 |17.5 |3018 |26.6 |130.16 |2.47 |52.7 |4.5 |0.019 | |80 |94.72 |17.5 |3009 |26.7 |130.14 |3.17 |41.05 |8.97 |0.059 | |125 |72.76 |17 |3009 |26.8 |128.25 |4.12 |31.13 |14.02 |0.111 | |171 |56.95 |17 |3000 |26.9 |128.23 |5.72 |24.33 |19.12 |0.161 | |212 |46.06 |16.5 |3006 |27.1 |126.28 |6.51 |19.40 |23.76 |0.202 | |232
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Discussion Our results indicate that the presence of iron increases the rate of the peroxidase’s activity‚ judging from the increase in absorbance with increasing amount of iron. This result supports our hypothesis that the iron acts as a cofactor in peroxidase’s activity and results in the faster rate of the reaction. Also‚ we assumed that the more we put iron in the solutions‚ the faster the rate is. This assumption is also supported by the results that higher concentration of iron cofactors shows
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