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.
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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.
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- Result and Discussion: Pauly Reaction: Samples: tyrosine, alanine, histidine Reagents: Cold Saturated Sulfanilic Acid, Cold 1 % Sodium Nitrite (NaNO2) and 10% Sodium Bicarbonate (Na2CO3) - Mix 0.5 ml of cold saturated sulfanilic acid solution (HANDLE WITH CARE) with 0.25 ml of cold 1.0% NaNO2. Cool in ice with constant shaking for 3 minutes. Add 0.5 ml of the sample and make alkaline with 10% Na2CO3. Record your observation.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…calculate the reaction velocity at saturating substrate concentrations. Your numerical answer is assumed to be in units of M sec-1. [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμM
- Give two advantages and two disadvantages to using the biuret reaction to measure protein concentration compared to measuring the protein absorbance directly at 280 nmDilution factor problem in buffer and unbuffered solution in enzyme. In factors affecting enzyme activity (pH, temeprature). In testing pH factors, 2% of 4 mL of unbuffered starch solution was added to 4 mL of buffered starch solution, plus the 2mL enzyme solution. However, in testing temperature, 1% of 8 mL buffered starch solution was added to 2mL of enzyme solution. Why use different 1% and 2% starch concentration? My teacher said that in the pH part, upon adding the volumes, it will be diluted to 1%. i don't understand how he got it? If I use M1V1=M2V2, the answer is clearly not 1%. I am very confused. Thank you.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.
- Substrate Concentration (mol L1) Velocity (mM min-1) 2.500 0.588 1.000 0.500 0.714 0.417 0.526 0.370 0.250 0.256 Determine the values of Km and Vmax for the decarboxylation of a 훃-keto acid given the followingdata. You have to plot the graph by using excel and please include the scope of graphgive two disadvantages to using the biuret reaction to measure protein concentration compared to measuring the protein absorbance directly at 280 nm.Give two advantages to using the biuret reaction to measure protein concentration compared to measuring the protein absorbance directly at 280 nm.
- Lab: Isolation of beta-amylase from sweet potato Objective: To isolate the enzyme β -amylase using sweet potato as a source Materials Required: Sweet potato.Knife/peeler.Mortar and Pestle.A Blender.Blue capped tubes.20mM sodium Phosphate buffer at pH 7.Vortexer. Procedure: 1.Take a clean sweet potato and peel the skin off.2.Weigh the peeled sweet potato and note the weight.3.The sweet potato is cut into small pieces and transferred into a mortar and pestle.4.The pieces are crushed and then transferred into a blender.5.Add 40 ml of cold 20mM sodium phosphate buffer saline. Blend it until it forms a paste.6.Gently transfer the potato slurry into a blue capped tube.7.Allow the enzyme to extract over a 1 hour period at room temperature, with frequent vigorous stirring on a vortex mixer.8.Then the extract is filtered using a GF A glass fibre filter and the filtrate is collected in a new blue capped tube.9.Centrifuge the filtrate at 12000rpm for 20 minutes at 4 degree Celsius.10. After…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?32. Between the following 4 Km values, select the one that indicates binding of the enzyme to its substrate with the highest affinity: Group of answer choices 10 nM 1000 uM 1 mM 10 pM