7.0, each into e 2 in ne ding 1. Du kan 8 10 6 itions. TABLE 2 Effect of pH on the Hydrolysis of Starch Time (Minutes) 3.0 7.0 0 73 73ba73 W 73 73 1.930 73 73 73 2 4 73 73 73 73 73 7 ining buffered enzyme 11.0 3 1,070 0.747 مرد
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- Calculate your dilution strategyto make a 625 ng/mLHRP solution from a 12.5 μg/mL stock given the totalvolume of enzyme youwillneed for your condition this week. Note if you are testing pH, you only need to calculate one enzyme dilution because all other pHs will use the same strategy.please fill out the table I need it for lab tomorrow At the start of the lab, you will be given stock preparations of alkaline phosphatase and PNPP onice—keep them that way. You will also be instructed on the volume of enzyme solution to beadded to reaction mixtures. Typically, this lab uses 5 μl of enzyme dilution. Before the start of lab, calculate thevolumes in μl of each component you need to mix together for each of these samples.For all of the following assays, use the amount of enzyme noted above and vary the substrateconcentration. Use the following assay format and PNPP concentrations of 0.0, 0.20, 0.40, 0.60,0.80, and 1.0 mM. Calculate the volumes of the 100 mM PNPP stock solution and buffer (finalvolume of 1.00 ml) needed to get each of the substrate concentrations. A single blank tube, withalkaline buffer only, is sufficient, because PNPP has no absorbance at 405 nm.An enzyme has a maximal Velocity of 110.36 uM/s. At a substrate concentrationof 8.5 uM/s. What is Km in uM? Thank You!
- You are given as following : 20 µl pure LDH on ice, 2.0ml of 6mM NAD+, 2.0ml of 150mM lactate, and 0.14M CAPS buffer. LDH reaction cocktail has final concentration of 1mM NAD+ and 25mM lactate in 0.14M CAPS buffer. LDH activityis measured by mixing 10 µl of LDH sample and 990 µl LDH reaction cocktail before getting ∆A340/min reading on spectrometer. (a). Describe in detail how you would prepare for your LDH reaction cocktail including how to make dilutions.An enzyme is present at 100 nM (nanomolar) and has a Vmax value of 25 uM/s (micromolar/second). The Km for the substrate is 5.2 uM. What is the kcat value? Report your answer to three significant figures in units of 1/s.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.
- Q1. We plan a farge scale purification of enzyme using a packed colum of polyacrylamide beads. We obtain the following data, in a bed. of volume. 201t Volume Eiuted (iters) ‘Concentration (Arbitrary Units] 126 00073 40 00162 (maximum) Find the yieid at 150 lites eluted.Quantitative Estimation of Amino Acids by Ninhydrin http://vlab.amrita.edu/?sub=3&brch=63&sim=156&cnt=2 can u help me with question 2 of the assignment questions Based on the experimental data provided, estimate the amount of amino acid in the given unknown solution by Ninhydrin method. SI No. Volume of standard amino acid solution (ml) Amount of amino acid (µg) OD at 570nm 1 Blank 0 2 0.2 0.12 3 0.4 0.25 4 0.6 0.45 5 0.8 0.55 6 1.0 100 0.68 7 Unknown (0.5ml) 0.41An enzyme is present at 100 nM (nanomolar) and has a Vmax value of 25 uM/s (micromolar/second). The Km for the substrate is 5.2 uM. What is the initial velocity (V0) at a substrate concentration of 15.2 uM? Report your answer to three significant figures in units of uM/s.
- Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…An enzyme “happyase” catalyzes the reaction: sad to happy. For total enzyme concentration of 4 nM, the measured Vmax was 3.2 μM/S. What is the kcat for happyase ______ and what is its unit _____ (shown in fraction format, eg. M/S)Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of increasingsubstrate concentration on reaction velocity was measured.In experiment 2 the reaction mixtures were identical tothose in experiment 1 except that 0.1 mg of an unknowncompound was added to each tube. Plot the data accordingto the Lineweaver-Burk method. Determine the effect of theunknown compound on the enzyme’s activity. (Substrateconcentration is measured in millimoles per liter. Velocity ismeasured in the change in optical density per hour.)