Before Lab: Compare the structures below to the structure of the substrate. Which do you think would be the most effective inhibitor of alkaline phosphatase? Which do you think would be the least effective inhibitor of alkaline phosphatase? glyphosate citric acid MES buffer cyclamate cantharidin
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- Result nad Discussion Lead Acetate Reaction: Samples: lysine, cysteine, methionine Reagents: 10% Sodium Hydroxide (NaOH) and Lead Acetate Pb(CH3COO)2 -To 1 ml of the amino acid solution taken in a test tube, add few drops of sodium hydroxide (40%) and boil the contents for 5-10 mins over a bunsen burner. Cool the contents and add few drops of 10% Lead acetate solution and observe.Table 1 - Comparison of the effect of catechol concentration on the amount of product formed. Absorbance Potato extract Absorbance 0 mins after 30mins (2nd reading) (mL) 1st reading 1 Tube # la blank 2a 3a 4a 1 1 1 dH₂O Catechol (mL) (mL) 7 5 3 1 0 2 4 6 0.00 0.060 0.033 0-05-2 Q4) Give 2 reasons for adding dH₂O to these tubes in Table 1? Time for reading: 3:21 -0.11 Absorbance: Time for reading: 3.36 Q5) Tube la serves as a control, but why is this control needed? Absorbance: 0.197 Time for reading: 3.37 Based on the data from Table 1 answer these questions: Q1) What is the name of the enzyme found in potato extract? Answer: catechol Q2) What is the substrate? Answer: THO Q3) Name of product of this enzyme catalyzed reaction? Answer: Absorbance: 0.152 Time for reading: 3:39 Absorbance: . 166 ness Catechol Benzoquinone Subtract 1st from 2nd reading -0.01 0-137 0.11.19 0.119 Q6) Notice that your 1st absorbance reading in tubes 2a-4a are quite similar but it then becomes very different…What are the corresponding answers, respond briefly, site sources Enzyme; Triacylglycerol Lipase Enzyme Official Name (write N/A if not applicable) Enzyme Official Number (4 digits) Simple or Conjugated Enzyme (specify cofactor if applicable) Type of Reaction Catalyzed Substrate Optimum pH Optimum Temperature Function/s Disease (give 1 and describe briefly) Enzyme: Urease Enzyme Official Name (write N/A if not applicable) Enzyme Official Number (4 digits) Simple or Conjugated Enzyme (specify cofactor if applicable) Type of Reaction Catalyzed Substrate Optimum pH Optimum Temperature Function/s Disease (give 1 and describe briefly)
- Figure I shows the Michaelis Menten plot of initial reaction velocity (as percentage of Vmax) versus [S] (concentration) for the carbonic anhydrase reaction in the absence and presence of the inhibitor acetazolamide. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. 100 No inhibitor Acetazolamide 0.2 0.4 0.6 0.8 1 [S] (mM) Figure 1 (i) Compare Vmax and Km of the enzyme without inhibitor and in the presence of acetazolamide. Determine the type of inhibition shown by acetazolamide. Explain your answer. (ii) Name TWO (2) other types of inhibitions besides the inhibition shown by acetazolamide in Qla)(i). List down the kinetic properties of these inhibitions. Sketch a graph of I/V versus 1/[S] showing plots in the absence of an inhibitor and in the presence of the types of inhibitors mentioned in Qla)(ii). (iii) V (% of VmaxAcetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows the experimental curve of initial reaction velocity (as percentage of Vmax) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor 50 Acetazolamide 0.2 0.4 0.6 0.8 (S] (mM) Figure 2 (i) Compare the maximal velocities and Michaelis Menten constants of the enzyme in the absence and the presence of the inhibitor acetazolamide. Determine the nature of inhibition by acetazolamide. Explain your answer. (*"A JO %) AAcetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows the experimental curve of initial reaction velocity (as percentage of Vma) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor 50 Acetazolamide 0.2 0.4 0.6 0.8 [S] (mM) Figure 2 (i) Compare the maximal velocities and Michaelis Menten constants of the enzyme in the absence and the presence of the inhibitor acetazolamide. Determine the nature of inhibition by acetazolamide. Explain your answer. (ii) Name TWO (2) other types of inhibitions besides the inhibition shown by acetazolamide. Sketch a graph of V versus [S] showing curves in the absence of an inhibitor and in the presence of the types of inhibitors not shown by acetazolamide. ("AJO %) A
- Course : BiochemistryChapter : Amino acid metabolism In the catabolic reaction of amino acids, ammonia is produced as a side compound.Ammonia is so poisonous that it must be removed from the body in the form of urea.Please explaina. the reaction of amino acids with ketoglutarate to produce ammoniab. the urea cyclec. where do reactions a and b occur? Please write the answer on paper ( Handwriting )And provide pict with detail explanation because i want to learn every steps of the processThank youTable 4- Determination of the optimum pH of catechol oxidase enzyme Potato extract (mL) Tube # 2d 3d 4d 5d 6d 7d dH₂O (mL) 0 0 0 0 0 0 Catechol (mL) 6 6 6 6 6 6 pH buffer added 4mL pH 2 4mL pH 4 4mL pH 6 4mL pH 7 4mL pH 8 4mL pH 10 1 1 1 1 1 1 Absorbance (0 mins) A: 0.010 Start Time: 3:24 A: 0.008 Start Time: 3:34 A: 0.023 Start Time: 3:36 A: -0.006 Start Time: 3:36 0.018 A: Start Time: 3:36 A: 0.011 Start Time: 3:36 Absorbance (after 10 mins in 40°C water bath) -0.030 A: Take reading at: 3:44 A: 0.154 Take reading at: 3:46 A: 0-105 Take reading at: 3:46 A: 0-132 Take reading at: 3:46 A: 0.074 Take reading at: 3:46 A: 0.018 Take reading at: 3!46 Q15) What is the enzyme's optimum pH(s)? Answer: Q16) Use the difference between 2nd and 1st absorbance to support your conclusion for the optimum pH. Subtract Omin from 10min absorbance -0.04 0.0012 0.082 0.138 0.056 0.007Give two advantages and two disadvantages to using the biuret reaction to measure protein concentration compared to measuring the protein absorbance directly at 280 nm
- Course : BiochemistryChapter : Amino acid metabolism Ammonia obtained from N2 will be used by plants to form other carbon compound amino acids.The process of assimilation of ammonia into larger molecules generally uses two compounds, namely glutamine and glutamate. -Explain the two reactions above!-Explain also the reaction of the assimilation of ammonia to amino acids!1. Explain why the maximum initial reaction rate cannot be reached at low substrate concentrationsPredict or describe the absorbance or enzyme activity at: pH = 2 pH = 14 Explain your predictions 2. Explain why the maximum initial reaction rate cannot be reached at low substrate concentrations.Lab: Borneol to borneone using Oxone in the presence of NaCl Testing using KI We performed a chemical test to check that the oxidant was fully quenched. Explain how this test works chemically. Which chemical is responsible for the dark brown color that is indicative of a positive test, write down the chemical reactions involved in the process?