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- Chitinase is a protein that breaks down chitin, a primary component of the cell wall in fungi, scales in fish and exoskeletons of arthropods. The activity of chitinase extracted from a plant was shown to be optimum at pH 5. You were tasked to prepare 300 mL of 150 mM buffer solution for further analysis of the extracted chitinase. REAGENTS Ka 2.5M Acetic acid Solid NaOAc•3H2O [136.08g/mol] 1.76 x 10-5 2.5M NH3 Solid NH4Cl [53.49g/mol] 5.6 x 10-10 2.5M Lactic acid Solid sodium lactate [112.06g/mol] 4.0 x 10-5 5 M HCl 5M NaOH Pls show sol'ns 1. Given the following reagents, give the moles of each component (acid & base).2. What are the mass/volume of the components needed to prepare the buffer? 3. What will the pH of the buffer be if 1mL of 5 M NaOH was added?If catalase is tested with the biuret reagent, what would be the ideal result? Why? If catalase is mixed with heavy metals, will it increase its activity of H2O2, yes or no? Defend your answer.Lineweaver-Burk plots of enzyme kinetics for the reaction, S <-> P, has the following features: 1/v is zero when 1/[S] equals -40 liter mole^-1; 1/[S] is zero when 1/v equals 2.0 x 10^5 min mole^-1. What are the Vmax and Km? Vmax = 5 umol min^-1, Km = 2.5 mM? Vmax = 5 mmol min^-1, Km = 25 M? Vmax = 5 umol min^-1, Km = 25 mM? Vmax = 5 mol min^-1, Km = 2.5 mM? Vmax = 5 mol min^-1, Km = 25 mM?
- True or False Immobilization improves the stability of the enzyme. EnaLne, has a half-life of 10 days in free solution, but under identical conditions of temperature, pH, and medium composition, the measured half-life of a packed column is 30 days. The enzyme is immobilized in a porous sphere 5 mm in diameter.After determining the optimum pH, you are now tasked to determine the inhibitory effects of acarbose, a known anti-diabetic drug which acts an inhibitor of alpha-glucosidase, an intestinal enzyme that hydrolyzes starch to release glucose for absorption and energy usage of the body. You studied the rates of the enzyme at different glycogen concentrations with and without the presence of 0.10 mM acarbose. Below is the summary for this procedure. a) What is the Vmax, in arbitrary units, of the uninhibited reaction (without acarbose)? b) What is the KM , in mM, of the uninhibited reaction (without acarbose)? c) What is the type of inhibition?There are parts A-C for this picture included. A) What type of enzyme is Malate Dehydrogenase? choices: Hydrolase, Isomerase, Ligase, Oxideoreductase, Transferase, or Translocase B) Which of the following statements are true in biochemical standard conditions? There can be more than 1. Choices: The reaction is spontaneous since ∆G°' is positive The reaction is spontaneous since ∆G°' is negative The reaction is not spontaneous since ∆G°' is positive The reaction is not spontaneous since ∆G°' is positive The equilibrium favors products since K is greater than 1 The equilibrium favors reactants since K is greater than 1 The equilibrium favors products since K is less than 1 The equilibrium favors reactants since K is less than 1 The reaction is always at equilibrium C) If the concentration of Oxaloacetate is 10^7 times lower than the concentration of Malate D.,Is the reaction Spontanuous? Choices: No, because RTInQ is very positive Yes, because RTlnQ is very…
- 41. A 14 year old girl is admitted to the hsopital after taking an overdose of aspirtin. Her plasma salicylate concentration is measured every6 hours for the next 24 hours Hours Plasma Salicylate(mg/dL) 6 12 12 90 18 45 24 10 Which of the following is the most likely explanation for the initial salicylate kinettics observed in this patient (A) Decreased protein binding (B) Delayed Absorption (C) First orderf Elimination (D) impaired Renal Elimination (E) Zero-order eliminationSerum blood of a patient with dislipoproteinemia type 1 has milky appearance even in fasting. If serum stays at low temperature (40) for several hours fatty layer appears on its surface. What are the possible causes of these symptoms? To explain this, answer the questions and do the following tasks: a) what compounds of serum must be tested for that patient in biochemical lab? b) write the reaction which does not occur properly in patient’s blood; c) write down the schemes, explaining how the products of the previous reaction are used in adipose tissue and heart in healthy person 2 hours after a meal.To purify a given enzyme from a crude extract that contains it, fractional precipitations, exchange chromatography are successively tested ionic and exclusion chromatography, with the results shown in the following table: Volume of dissolution Protein concentration Enzymatic activity (ml) (mg/ml) (U/ml) a) Calculate the percentage of recovery of the enzyme after each of the manipulations to which it has been subjected. b) Indicate if it is necessary to continue purifying the enzyme or if it is expected to have reached its electrophoretic homogeneity.
- Acetocholinesterase is an enzyme possessing a single active site that metabolizesacetylcholine with a turn over number of 1.4 x 10^4s-1. How many grams of acetylcholine(molecular formula C7NO2H16+) will 2.16 x 10^-6 g acetocholinesterase metabolize in 60minutes? (The enzyme’s molecular mass is 4.2 x 10^4 g/mol).The concentration of hydrolyzed nitrocefin at each time point for an experiment is given below. Time (min) Concentration (μM) 0.5 6.01 1 11.78 1.5 17.6 2 23.51 2.5 29.58 3 35.31 3.5 39.73 4 44.5 4.5 48.18 5 50.05 5.5 52.72 6 54.01 6.5 55.06 7 55.65 7.5 56.39 8 56.74 8.5 57.49 9 58.03 9.5 58.61 10 58.69 Make a graph that plots the concentration of hydrolyzed nitrocefin (in μM) against time (in seconds) using Excel, R, SPSS or other computable software. Where appropriate, include a trendline that shows the linear range on your graph. Include the equations for the trendlines and the R2 value on the graph. Your graph should also include a title and appropriate titles for the x- and y-axes, with units included where appropriate. To determine the initial velocity of a possible insert in this experiment, you must determine what the linear range is in these data (see note below). Based on your graph, which time points represent a suitable linear…The turnover number for an enzyme that approximates Michaelis-Menten kinetics is known to be 500 min^-1. From the results shown in the table, enumerate Km and total amount of enzyme present. What is the Km for this enzyme? What is the Vmax for this enzyme? And what is the [E]T for this enzyme?
