Factor Control #1 (H202 + MnO2) Control #2 (H202 + sand) Plant vs Animal Catalase (Liver) Plant vs Animal Catalase (Potato) Concentration of Substance Enzyme (Used Liver) Concentration of Substance Enzyme (Used H202) Temperature: Boiling Water Bath Temperature: Ice Water Bath PH 3 (HCI) pH 12 (NaOH) pH 7 (H2O) Rate of Reaction 5 0 4 3 4 1 5 2 4 2 1 Graph A visual story of the correlation between variables Graph 1: Volume vs. Mass for Water at Room Temperature Mass (g) 110 Distilled, be descriptive Data points must be an x or a circled dot. This is incorrect. Slope is calculated on the graph replacing m, y and x with the symbols representing the variables of the graph and what the slope is calculating. A triangle on the line of best fit, largely drawn to reduce error, indicates the data used in the calculation. The triangle does not use 0,0 because this is not experimental data. 100 90 80 70 60 50 40 30 20 10 0 0 10 20 30 40 50 60 70 80 Volume (mL) 90 100 110 paper and half the page minimum size Must be on grid The independent variable is on the X axis with the dependent variable on the y axis

Factor Control #1 (H202 + MnO2) Control #2 (H202 + sand) Plant vs Animal Catalase (Liver) Plant vs Animal Catalase (Potato) Concentration of Substance Enzyme (Used Liver) Concentration of Substance Enzyme (Used H202) Temperature: Boiling Water Bath Temperature: Ice Water Bath PH 3 (HCI) pH 12 (NaOH) pH 7 (H2O) Rate of Reaction 5 0 4 3 4 1 5 2 4 2 1 Graph A visual story of the correlation between variables Graph 1: Volume vs. Mass for Water at Room Temperature Mass (g) 110 Distilled, be descriptive Data points must be an x or a circled dot. This is incorrect. Slope is calculated on the graph replacing m, y and x with the symbols representing the variables of the graph and what the slope is calculating. A triangle on the line of best fit, largely drawn to reduce error, indicates the data used in the calculation. The triangle does not use 0,0 because this is not experimental data. 100 90 80 70 60 50 40 30 20 10 0 0 10 20 30 40 50 60 70 80 Volume (mL) 90 100 110 paper and half the page minimum size Must be on grid The independent variable is on the X axis with the dependent variable on the y axis

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Materials - 2021FA-CHM-1O X Bb 4427577 d-fleet02-xythos.content.blackboardcdn.com/6086c260d7e8f/4427577?X-Blackboard-Expiration=1633143600000&X-Blackboard-Sig 6 / 9 100% Exercise 1: Standard Curve for Protein Measurements: A standard curve for protein concentration is often created using known concentrations of bovine serum albumin (protein). This process is called the Bradford Assay; it is a colorimetric assay. A special reagent turns blue when it binds to amino acids present in protein. The intensity of the color is best measured with a spectrophotometer (a device for comparing two light radiations, wavelength by wavelength). In the case of the Bradford Assay the greater the absorbance, the higher the protein concentration. A series of tests were performed on some samples and spectrophotometer: following measurements were obtained using a Protein Concentration (mg/ml) Absorbance (A) 0.26 0.098 0.56 0.213 0.383 0.84 1.12 0.473 1.40 0.527 TASKS: 1. Enter the data into Excel - the…
What is the Posner task? Describe its purpose and setup (materials, conditions, etc.). What do its results (graph pictured here) indicate, and why? Reaction time (msec) 300 250 200 Invalid Neutral Valid Cue
Concentrations in biochemical systems are often very dilute. Consequently, scientific notation and logarithms are often used to express concentrations. In scientific notation, numbers are expressed as coefficient x 10" To convert a number to scientific notation, proceed as follows: 1. Move the decimal place so that there is one digit in front of the decimal. 2. Account for the moved decimal in the value of x. If the decimal moved to the right, x is negative; if it moved to the left, x is positive. A logarithm is basically an exponent. Unless otherwise indicated, a logarithm is the a of 10". The numbers after the decimal point are significant; the number before the decimal just identify the location of the decimal point for the number. Notice that it is easy to estimate a logarithm from scientific notation; it's the exponent! Logarithms are commonly used to express the concentration of H. The pH is defined as pH= log (In), where the base number is 2.303. The same general rules as logs…
Table 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 0.007
Part 1: Assess the following partial results section below by editing it for brevity by omitting any unnecessary parts (1 point), explain why you decided to remove certain sections (1 point): To evaluate inhibitory effects of the selected molecules, 10mM stock solutions of each molecule were prepared in DMSO. A reaction mixture (200μl) was prepared with the same formula optimized for the enzyme activity assay (0.1 M Tris-HCl ph 8, 0.1 M KCI, 25 mM NaCl, 0.25 mM ATP, and two units of inorganic yeast pyrophosphatase) with 10 µM of the sample molecule. The reaction mixture was incubated for 20 minutes at ambient temperature. Enzymatic reaction was triggered by addition of the substrate B (0.2 mM) and the absorbance of the product was monitored at 290 nm for 10 minutes. Six out of 15 sample molecules showed appreciable inhibition at 10 μM (Figure 5). Three of the molecules, A3, A6, and A7 exhibited more than 50% inhibition of the enzyme activity and were further diluted to find the minimal…
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).
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.
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A biochemist discovers and purifies a new enzyme, generating the purification table below. Procedure Total Protein (Mg) Activity (Units) Crude Extract 20,000 4,000,000 Precipitation (Salt) 5,000 3,000,000 Precipitation (pH) 4,000 1,000,000 Ion Exchange Chromatography 200 800,000 Affinity Chromatography 50 750,000 Size-exclusion Chromatography 45 675,000 a) From the information given in the table, calculate the specific activity of the enzymeafter each purification procedure.b) Which of the purification procedures used for this enzyme is most effective (i.e., givesthe greatest relative…
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Using G-25 Sephadex beads (Fractionation range 1000-5000) KD, a sample of Vitamin B12 (MW ~1500 KD) will be: Partially included Fully excluded Fully included
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