Sketch the following five graphs and label them clearly. A) hemoglobin a subunit in the presence and absence of BPG at l...
Sketch the following five graphs and label them clearly.
A) hemoglobin a subunit in the presence and absence of BPG at low pH
B) hemoglobin in the presence of BPG at low and high pH
C) myoglobin and hemoglobin a subunit in the presence at low pH
D) myoglobin and hemoglobin in the presence at high pCO2
E) an enzyme with no inhibitor, in the presence of a competitive inhibitor, and in the presence of a non competitive inhibitor
Homework Answers
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Sketch the following five graphs and label them clearly. A) hemoglobin a subunit in the presence and absence of BPG at l...
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor....
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed non-competitive kinetics with y- intercepts of 15s -1 and 5 s -1 in the presence and absence of the inhibitor respectively. If the inhibitor binding constant was 0.5nM, calculate [I ] used in this reaction? a. 0.135nM b. none of the above c. 0.225nM d. InM e. 0.125nM
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor....
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed competitive kinetics with x-intercepts of -10mm -1 and -3.5mm -1 in the presence and absence of the inhibitor respectively. If the inhibitor concentration used was 2micro molar (UM), calculate KI for the inhibitor enzyme binding? a. none of the above b. 0.135nM c. 0.054nM d. 0.225nM e. 1077 nM
how did they get these answers? we Vulins Hemoglobin/Am 1. An allosteric interaction between a) binding of a molecul...
how did they get these answers?
we Vulins Hemoglobin/Am 1. An allosteric interaction between a) binding of a molecule to a bir 0 You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data are obtained: [S] Vo -Inhibitor +Inhibitor 17 29 0.0001 0.0002 0.0005 0.001 0.002 0.005 0.01 0.02 0.05 0.1 100 100 100 98 99 100 100 0.2 a) What is the Vmax...
2) We discussed in class how the molecule 2,3-bisphosphoglycerate (BPG) is an inhibitor of hemoglobin (Hb)....
2) We discussed in class how the molecule 2,3-bisphosphoglycerate (BPG) is an inhibitor of hemoglobin (Hb). Answer the following questions about BPG and its regulation of oxygen binding: a) Would BPG have any effect on myoglobin’s ability to bind or release oxygen? If so, describe how BPG would affect myoglobin. If not, why? b) Based on the observation that BPG binds preferentially to partially deoxygenated Hb, briefly explain (1-2 sentences) where BPG is most likely to be most effective on...
i need help with part two PART TWO 1) The steady-state kinetics of an enzyme is studied in the absence and presence...
i
need help with part two
PART TWO 1) The steady-state kinetics of an enzyme is studied in the absence and presence of inhibitor A. The initial rate is given as a function of substrate concentration in the following table. [S] (MM) * Velocity in substrate only y (mM/min) .25 1.72 58 ,598 r.60 2.04 .44 50 A 2.63 238 5.00 .2 3.33 10.00 4.17 4 Velocity in substrate + S inhibitor A (MM/min) 0.98 1.02 | 1.17 . 5...
i need help with part two the open ended section Patients with chronic hypoxia (low 0, levels) due to decreased lung...
i
need help with part two the open ended section
Patients with chronic hypoxia (low 0, levels) due to decreased lung function may adapt by increasing their circulating BPG levels, Predict which outcome will be TRUE for such a patient. "A) The R-state of hemoglobin will be favored. B) O, binding to hemoglobin will be hyperbolic. C) Pse for O2 will be increased D) Pse for O2 will be decreased. B) None of the answers is correct. 14. Which amino...
biochemistry concept I need help with. not a hw question. on our test our professor is...
biochemistry concept I need help with. not a hw question.
on our test our professor is going to ask us something along
the lines of these questions but I just don't understand them even
after reading the questions. I don't understand how to know when to
shift the line to the right vs left.
HEMOGLOBIN Draw the oxygen-binding curve on the graph for A-normal hemoglobin, B normal hemoglobin when BPG levels double and c-a disease that causes high blood oxygenation...
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of...
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of an inhibitor at 5 mM concentration (2). Assume[ET] is the same in each experiment. [S] (MM) (1) v(umol/mL sec) 12 (2) v(umol/mL sec) 4.3 1 8 2 4 20 29 14 21 8 35 12 40 26 a. Using a graphing program (excel or sigmaplot) construct a lineweaver burke plot representing the uninhibited reaction and the inhibited...
61. Which of the following promotes the unloading of O2 from hemoglobin in the tissues? a....
61. Which of the following promotes the unloading of O2 from hemoglobin in the tissues? a. the relatively low concentration of CO2 b. the relatively high pH d. the fact that the tissues are hypertonic c. the relatively low concentration of O2 e. none of the above 62. Which of the following promotes the loading of O2 onto hemoglobin in the lungs? a. the relatively high concentration of CO, b. the relatively low pH d. the fact that the lungs...
41. Which of the following statements about protein-ligand binding is correct? A) The K is equal...
41. Which of the following statements about protein-ligand binding is correct? A) The K is equal to the concentration of ligand when all of the binding sites are occupied. B) The K is independent of such conditions as salt concentration and pH. C) The larger the K. (association constant), the weaker the affinity. D) The larger the K. the faster is the binding. E) The larger the K, the smaller the K. (dissociation constant) 42. The ability of O, to...
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed non-competitive kinetics with y- intercepts of 15s -1 and 5 s -1 in the presence and absence of the inhibitor respectively. If the inhibitor binding constant was 0.5nM, calculate [I ] used in this reaction? a. 0.135nM b. none of the above c. 0.225nM d. InM e. 0.125nM
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed competitive kinetics with x-intercepts of -10mm -1 and -3.5mm -1 in the presence and absence of the inhibitor respectively. If the inhibitor concentration used was 2micro molar (UM), calculate KI for the inhibitor enzyme binding? a. none of the above b. 0.135nM c. 0.054nM d. 0.225nM e. 1077 nM
how did they get these answers?
we Vulins Hemoglobin/Am 1. An allosteric interaction between a) binding of a molecule to a bir 0 You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data are obtained: [S] Vo -Inhibitor +Inhibitor 17 29 0.0001 0.0002 0.0005 0.001 0.002 0.005 0.01 0.02 0.05 0.1 100 100 100 98 99 100 100 0.2 a) What is the Vmax...
i
need help with part two
PART TWO 1) The steady-state kinetics of an enzyme is studied in the absence and presence of inhibitor A. The initial rate is given as a function of substrate concentration in the following table. [S] (MM) * Velocity in substrate only y (mM/min) .25 1.72 58 ,598 r.60 2.04 .44 50 A 2.63 238 5.00 .2 3.33 10.00 4.17 4 Velocity in substrate + S inhibitor A (MM/min) 0.98 1.02 | 1.17 . 5...
i
need help with part two the open ended section
Patients with chronic hypoxia (low 0, levels) due to decreased lung function may adapt by increasing their circulating BPG levels, Predict which outcome will be TRUE for such a patient. "A) The R-state of hemoglobin will be favored. B) O, binding to hemoglobin will be hyperbolic. C) Pse for O2 will be increased D) Pse for O2 will be decreased. B) None of the answers is correct. 14. Which amino...
biochemistry concept I need help with. not a hw question.
on our test our professor is going to ask us something along
the lines of these questions but I just don't understand them even
after reading the questions. I don't understand how to know when to
shift the line to the right vs left.
HEMOGLOBIN Draw the oxygen-binding curve on the graph for A-normal hemoglobin, B normal hemoglobin when BPG levels double and c-a disease that causes high blood oxygenation...
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of an inhibitor at 5 mM concentration (2). Assume[ET] is the same in each experiment. [S] (MM) (1) v(umol/mL sec) 12 (2) v(umol/mL sec) 4.3 1 8 2 4 20 29 14 21 8 35 12 40 26 a. Using a graphing program (excel or sigmaplot) construct a lineweaver burke plot representing the uninhibited reaction and the inhibited...
61. Which of the following promotes the unloading of O2 from hemoglobin in the tissues? a. the relatively low concentration of CO2 b. the relatively high pH d. the fact that the tissues are hypertonic c. the relatively low concentration of O2 e. none of the above 62. Which of the following promotes the loading of O2 onto hemoglobin in the lungs? a. the relatively high concentration of CO, b. the relatively low pH d. the fact that the lungs...
41. Which of the following statements about protein-ligand binding is correct? A) The K is equal to the concentration of ligand when all of the binding sites are occupied. B) The K is independent of such conditions as salt concentration and pH. C) The larger the K. (association constant), the weaker the affinity. D) The larger the K. the faster is the binding. E) The larger the K, the smaller the K. (dissociation constant) 42. The ability of O, to...
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