BIOL 1107L Starch Analysis Results (2)

Example of a Protein Purification Scheme: Purification of the Enzyme Xanthine Dehydrogenase from a Fungus Volume Total Total Specific Percent Fraction (mL) Protein (mg) Activity Activity Recovery 1. Crude extract 2. Salt precipitate 3. Ion-exchange chromatography |4. Molecular-sieve chromatography 5. Immunoaffinity chromatography 3,800 22,800 2,460 0.108 100 165 2,800 1,190 0.425 48 65 100 720 7.2 29 40 14.5 23 1.8 275 152.108 11 Calculate the specific activity of step#4. Note that percent recovery=% Yield.

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?

y biochemical calculation w linear regression parameters. please write complete values and answer all

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Paper electrophoresis of Asn, Ala, Asp, Lys and Ser mixtures at pH = 7 shows the fastest movement towards the anode The fully saponified 10g oil sample consumed 1.87g KOH, and the iodine value of the oil was 28.3. So how many unsaturated double bonds are there in each oil molecule on average? (lodine is known to have an atomic weight of 127) Given that 100g cellulose sample is completely hydrolyzed to obtain 78g glucose, then the percentage of cellulose in the sample is _% Given that the Km of catalase is 20mmol/L and the substrate concentration is 80mmol/L, then the percentage of catalase bound to the substrate is %

suctose density gradient ultractifugation is a powerful technique for fractionating macromolecules like DNA,RNA and proteins.some protocols using sucrose gradients mention the following:10 mL sucrose gradients 10-15%(w/v) in 10 mM HEPES buffer.How would you prepare this sucros gradient?

Given the information and table pls answer the question.Protein XYZ is a heme-containing protein responsible in electron transfer in microalgae. The target protein was extracted using ammonium sulfate fractional precipitation and quantified using Bradford assay. A set of solutions with increasing concentration was prepared using 15.00 mg/mL analogous protein standard [refer to succeeding table]. Each solution was treated with 80 μL of Bradford reagent and diluted to 1.500mL. The absorbance at 595 nm of each solution was obtained and presented below.A 2-mL aliquot of the crude extract was diluted to 10mL with distilled water. The absorbance at 595 nm of this solution was obtained to be 1.1340. Thus, further dilution of the crude extract solution was performed. Two milliliters of the previously diluted solution was treated with 8 mL of distilled water. The absorbance of the final solution at 595 nm was determined to be 0.2150.What is the concentration (in mg/mL) of Protein XYZ in the…

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8L.Part I

Hand draw the expected gel result from the graphical data of three extracted RNA samples (in Figure 1a, 1b, & 1c) in Nanodrop spectrophotometer. The 3 graphical data should be in 1 agarose gel Provide complete gel label descriptions (ladder, lanes, etc.).

Calculate how much agarose is needed to make a 3% agarose gel in a volume of 150 ml 1x TAE buffer.

National Board of Medical Examiners Biochemistry Mark 36. In the presence of a metabolite (X), 6-phosphofructokinase is assayed at a fixed concentration of ATP and varying concentrations of fructose 6-phosphate. The resulting data are shown in the table. Fructose 6-phosphate (pM) 5 10 20 40 75 100 200 Velocity umoles/min 0.05 0.15 0.25 0.70 1.7 2.2 3.1 3.1 Velocity (+X) umoles/min 0.006 0.025 0. 10 0.35 1.03 16 2.9 3.1 400 Metabolite (X) is most likely which of the following substances? O A) ADP O B) AMP OC) CAMP D) Citric acid O E) Fructose-2,6-bisphosphate

Hi I need help finding the independent and dependent variable for my data. Thank you.

You want to prepare 500 mL of the macronutrient and micronutrient stock solutions which have 100X and 1000X higher concentration, respectively, than the required concentration in the culture mediuma)If 0.17 g/L KH2PO4 is required in MS medium, determine the mass (g) of KH2PO4 that is required to prepare the stock solution and the volume required (mL) to prepare 200 mL MS medium. Show your work.

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Calculate the Activity of an amylase enzyme  which is diluted 1:100 times with phosphate buffer and incubated for 10 minutes at 37 degree Celsius. Given are the amount of maltose [mg] = 5.05 and the volume of enzyme used for the assay as 0.5ml.

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A purified protein sample was used in a reaction, resulting in an activity of 696.7 nmol min-1. The reaction volume was 145.0 µL and the final volume before loading the plate was 1,050 µL. The total reaction time was 4.25 min. The amount of protein used in the reaction was 4.270 µg. Calculate the specific activity of the sample (in nmol min-1 µg-1).

Hello! Can you please help me with the following: a.    Draw the basic batch growth curve and label the four difference phases of growth and kinetics on the curve.b.    Give a description of each phase on the curvec.    Compare (less than, greater than, equal to, equal to zero) growth rate (Rg) and death rate (Rd) at each phase.d.    What is the deceleration phase? Where is this phase on the curve (circle the location)?e.    What does it mean that the exponential growth phase is 1st order? Please give the equation that represents the order of the exponential growth phase.  Thank you!

Various concentrations of recombinant human insulin were prepared for use standards for an HPLC method. To verify the prepared concentrations, the samples were analyzed by measuring the absorbance at 280 nm in a short path length (5 mm) cuvette. The molar absorption coefficient for human insulin is approximately 5.875 x 10³ M-¹cm-¹. a. Calculate the extinction coefficient in mL mg-¹cm-¹. b. Calculate the concentrations of the following human insulin standards if the measured absorbances and dilutions used are: Standard 1 Standard 2 Abs. (at 280 nm) of Diluted Sample 0.305 0.685 Dilution 145.0 µL sample, 25.0 μL buffer 130.0 µL sample, 40.0 μL buffer

RESTRICTION ENZYME MAPPING Predict the result

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