14 A kinetic study of an intestinal peptidase using glycylglycine as the substrate produced the experimental data shown in the table.glycylglycine + H,O -2 glycine[S] (mM)Product formed (umol min)1.50.212.00.243.00.284.00.338.00.4016.00.45Calculate the standard error of regression (SER) for the Lineweaver-Burk slope and the Eadie-Hofstee slope to compare theprecision of cach.umol min"Lineweaver-Burk SER:umol min-Eadie-Hofstee SER: 84.5%ResourcesO HintCheck AnsweThere are several ways to transform the Michaelis-Mentenequation so as to plot data and derive kinetic parameters, cachwith different advantages depending on the data set beinganalyzed. One transformation of the Michaelis-Mentenequation is the Lineweaver-Burk, or double-reciprocal,equation. Multiplying both sides of the Lineweaver-Burkequation by Vmax and rearranging gives theEadie-Hofstee equation.Slope = -KVo+ Vmax[S]Vo = - (K)Vofor an enzyme-catalyzed[S]Consider the plot of Va versusreaction. The control reactions (blue curve) did not containany inhibitor.[S]Which of the other curves (A, B, or C) depicts this enzyme's activity in the presence of a competitive inhibitor?curve Acurve Ccurve B

Hi! Since you have posted multiple questions we will answer the first question for you. Kindly…

Answered: A kinetic study of an intestinal…

Biochemistry

9th Edition

ISBN:9781305961135

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

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

Chapter15: The Importance Of Energy Changes And Electron Transfer In Metabolism

Section: Chapter Questions

Problem 11RE

See similar textbooks

Similar questions

MATHEMATICAL The standard free-energy change for the reaction Arginine+ATPPhosphoarginine+ADP is +1.7kJmol1. From this information and that in Table 15.1, calculate the G for the reaction Phosphoarginine+H2OArginine+Pi
MATHEMATICAL The enzyme -methylaspartase catalyzes the deamination of -methylaspartate [V. Williams and J. Selbin, J. Biol. Chem. 239, 1636 (1964)]. The rate of the reaction was determined by monitoring the absorbance of the product at 240 nm(A240). From the data in the following table, determine KM for the reaction. How does the method of calculation differ from that in Questions 26 and 27?
RECALL For the reaction of glucose with oxygen to produce carbon dioxide and water, Glucose+6O26CO2+6H2O the DG is 22880 kJ mol-1, a strongly exergonic reaction. However, a sample of glucose can be maintained indefinitely in an oxygen-containing atmosphere. Reconcile these two statements.
(Biochemistry) Discuss the factors that affect the 260/280 ratio.
Biomaterial question: Give a brief and clear answer, please Sketch a typical stress-strain curve for three major types of biomaterials. Describe Young’s modulus and write Hooke’s Law. What are the time-dependent properties of materials? Explain briefly.
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?
Ethylene oxide is produced industrially from the reaction of ethylene with oxygen at atmospheric pressure and 277 oC, in the presence of silver catalyst.C2H4(g) + O2(g) → C2H4O(g) (unbalanced)Assuming 100 % yield, how many kg of ethylene oxide can be produced from 34600 L of a mixture containing ethylene and oxygen in 1:1 molar ratio?
The turnover number for an enzyme that approximates Michaelis-Menten kinetics is known to be 500 min^-1. From the results shown in the table, enumerate Km and total amount of enzyme present. What is the Km for this enzyme? What is the Vmax for this enzyme? And what is the [E]T for this enzyme?
MATHEMATICAL The buffer needed for Question 35 can also be prepared using crystalline NaH2PO4 and a solution of 1.0 M NaOH. How would you do this?
The Keq (25C) of the reaction below is 635.67. Fructose 1,6-biphosphate <-->fructose -6-phosphate + Pi. a) What is the standard Gibbs free energy change for this reaction? b) if the concentrationof fructose 1,6 biphosphate is adjusted to 0.85 M and that of fructose 6 phosphate and phosphate adjusted to 0.055 M, what is the actual free energy change
For an enzyme that displays Michaelis-Menton kinetics, what is thereaction velocity, V (as a percentage of V max , observed at the followingvalues?[S] = K M[S] = 0.5K M[S] = 0.1K M[S] = 2K M[S] = 10K M
Nonspecific elution of affinity bonded macromolecules is used in affinity chromatography explain why?

SEE MORE QUESTIONS

Recommended textbooks for you

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

Principles Of Pharmacology Med Assist

Biology

ISBN:

9781337512442

Author:

RICE

Publisher:

Cengage

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

Principles Of Pharmacology Med Assist

Biology

ISBN:

9781337512442

Author:

RICE

Publisher:

Cengage

SEE MORE TEXTBOOKS