i need the answer quickly 2) Two students attempted to estimate the extinction co-efficient of NADH by measuring theabsorbance of different concentrations at 340nm. The data was plotted and a linear regression fitted0.350.30Replicate 1:Absorbance = 6.32 x [NADH] (mM)0.250.200.150.100.05Replicate 2:Absorbance = 2.80 x [NADH] (mM)0.000.000.010.020.030.040.050.06NADH concentration (mM)Figure 1: Estimation of the extinction co-efficient of NADH. The absorbances of differentconcentrations of NADH were measured at 340nm. Linear regressions were fitted to the two datasets, with the equations displayed.i) Describe the differences between the two replicate standard curves.ii) Speculate on a possible reason that may explain the differences between the two replicates?"Absorbance (340nm)

The amount of light absorbed by a sample is known as its optical density which can be determined by…

Answered: 2) Two students attempted to estimate…

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

See similar textbooks

Similar questions

What is the change in concentration (umol/mL/min) for NADPH if the change in absolute absorbance per second from your DHFR functional assay analysis was 0.0035?
Consider the following experimental data from another experiment: [S] 1.5 2.00 2.50 5.00 10.00 V (No inhibitor) mmol ml¹ min¹ 0.167 0.204 0.232 0.313 0.385 V (inhibitor) mmol ml¹¹ min¹¹ 0.115 0.143 0.167 0.250 0.333 Calculate Km and V max and determine whether this inhibitor is competitive, non-competitive or uncompetitive.
calculate the actual free energy of hydrolysis of ATP, delta Gp in the erythrocytes of a new species. The standard free-energy of hydrolysis of ATP is also -30.5kJ/mol in this species, but the concentrations in this specie's erythrocytes are 0.00775 mM ATP, 0.00027 mM ADP and 0.00418 mM Pi. Assume the pH is 7.0 and the body temperature of this species is 43.0oC. Calculate your answer as kJ/mol to two decimal places.
In vitro experiments are conducted at pH = 7.4 to simulate physiological conditions. A phosphate buffer system is often used. H₂PO → H₂PO¹²¯ +H+ pK₁ = 7.2 a. What must be the ratio of the concentrations of HPO to H₂POд ions? b. What mass of NaH2PO4 must be added to 500.0 mL of 0.10 M Na₂HPO4 (aq) in the preparation of the buffered solution?
Calculate the reduction potential of cytochrome a3 (°' = 0.385 V) at 25.0°C when the Fe3+ form = 87.0 μM and the Fe2+ form = 25.0 μM. 0.440 V 0.353 V 0.417 V 0.387 V
Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the above enzyme (lactase). (enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM) 0.125 per minute 0.25 per minute 0.50 per minute 1.25 per minute 5.0 per minute
Acetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows the experimental curve of initial reaction velocity (as percentage of Vmax) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor 50 Acetazolamide 0.2 0.4 0.6 0.8 (S] (mM) Figure 2 (i) Compare the maximal velocities and Michaelis Menten constants of the enzyme in the absence and the presence of the inhibitor acetazolamide. Determine the nature of inhibition by acetazolamide. Explain your answer. (*"A JO %) A
Calculate for the water activity of the soy sauce in 80.3% ERH. Suppose the soy sauce is subjected to a storage area with RH of 95.9%. What will be the water activity of the soy sauce?
Acetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows the experimental curve of initial reaction velocity (as percentage of Vma) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor 50 Acetazolamide 0.2 0.4 0.6 0.8 [S] (mM) Figure 2 (i) Compare the maximal velocities and Michaelis Menten constants of the enzyme in the absence and the presence of the inhibitor acetazolamide. Determine the nature of inhibition by acetazolamide. Explain your answer. (ii) Name TWO (2) other types of inhibitions besides the inhibition shown by acetazolamide. Sketch a graph of V versus [S] showing curves in the absence of an inhibitor and in the presence of the types of inhibitors not shown by acetazolamide. ("AJO %) A
In a photosynthetic investigation, a student measured the following pH of the stroma and the inner thylakoid compartments of spinach leaf cells at the conclusion of the experiment. Source of Fluid pH (mean) Standard Error of Mean (SEM) Stroma 8.2 0.75 Inner compartment of thylakoid 5.6 0.35 b. Construct an appropriately labeled graph to illustrate the sample means of the two locations to within 95% confidence (i.e. sample mean + 2 SEM).
Calculate the Vmax of the above enzyme (lactase). (the enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM) 0.125 mM per minute 0.25 mM per minute 0.50 mM per minute 1.25 mM per minute 5.0 mM per minute
The temperature dependence of the vapor pressure is given by the equation: ΔΗ RT Inp = In A – Where: p= vapor pressure T = temperature A = pre-exponential constant AHvap = enthalpy of vaporization In order to solve for the enthalpy of vaporization, AHvap, you must: Step One Add the same expression to each side of the equation to leave the term that includes the variable by itself on the right-hand side of the expression: (Be sure that the answer field changes from light yellow to dark yellow before releasing your answer) ΔΗ RT + Inp = + In A Drag and drop your selection from the following list to complete the answer: 1 1 In In A - In A K

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS