Carbon monoxide competes with 02 binding by hemoglobin, and exposure can lead to toxicity. Could carbon monoxide be considered an allosteric effector? O No since the it competes for the active site of the molecule O Yes because it will reduce 02 binding O Yes since the it competes for the active site of the molecule O No because it will reduce 02 binding and is a negative effector

Carbon monoxide competes with 02 binding by hemoglobin, and exposure can lead to toxicity. Could carbon monoxide be considered an allosteric effector? O No since the it competes for the active site of the molecule O Yes because it will reduce 02 binding O Yes since the it competes for the active site of the molecule O No because it will reduce 02 binding and is a negative effector

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter11: The Blood

Section: Chapter Questions

Problem 1SQE

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Similar questions

Carbon monoxide competes with hemoglobin for 02 binding, resulting in toxicity. Is it possible that carbon monoxide is an allosteric effector? No, since it competes with the molecule O for the active site. Yes, since it will minimize the amount of 02 binding. O Yes, since it competes with the molecule O for the active site. No, since it is a negative effector that reduces 02 binding.
Which among the following statements is correct? Negatively-charged proteins are eluted out first when a cation exchanger is used as the stationary phase for ion- exchange chromatography O Proteins that have higher affinity to the ligands are eluted out last in affinity chromatography O Both statements are correct O Both statements bre incorrect
Allosteric inhibitors of hemoglobin will decrease enzyme activity (oxygen binding) through which of the following mechanisms? Binding the enzyme in "T" conformation and displacing an activator Binding the enzyme and enhancing the Vmax Binding the enzyme, and keeping it in the "R" conformation Binding the enzyme, and keeping it in the "T" conformation
The Graph below shows the binding curves of two proteins (A and B) for the same ligand (L). Use this Graph and determine the dissociation constant, K, for both proteins. Which protein (A or B) has a greater affinity for ligand L? Which of the two proteins would be more easily inhibited by an antagonist? 1.0 Y 0.5 2 A 4 6 B 8 [L] (μM) 10 12 14 16
The following structure is more active than morphine as an analgesic. H3C N. CH3 H. H3C O .. What is the principal reason for this? O The extra acetyl group binds to cell surface receptors improving active internalization. O The acetyl groups mask a polar group allowing the structure to cross the blood brain barrier more efficiently. O The extra acetyl group masks an alcohol group which would otherwise undergo a phase Il metabolic conjugation reaction leading to rapid excretion of the drug. O The acetyl groups increase the stability of the drug in the cellular environment. O ..
The following structure is more active than morphine as an analgesic. H3C CH3 H. H3C' O Il.. What is the principal reason for this? The extra acetyl group binds to cell surface receptors improving active internalization. The acetyl groups mask a polar group allowing the structure to cross the blood brain barrier more efficiently. The extra acetyl group masks an alcohol group which would otherwise undergo a phase Il metabolic conjugation reaction leading to rapid excretion of the drug. The acetyl groups increase the stability of the drug in the cellular environment. O Il..
In addition to O, binding, changes in other chemical conditions can result in hemoglobin changes. pH is one of those factors. It can be understood by reaction #1. Red blood cells have the enzyme Carbonic Anhydrase which catalyzes reaction #2. Using the two reactions explain how pH contributes to the transfer of O2 from the lungs to the tissues. H-Hb* + O2 Hb-O2 + H* Reaction #1 CO2(aq) + H2O= H* + HCO3 Reaction #2
A mutation of Lysine 82 (in the DPG-binding pocket) to Arginine in beta sub-unit will most likely result in Not enough information Higher than normal binding affinity to oxygen Lower than normal binding affinity to oxygen Normal binding to oxygen
Why is salbutamol better than isoproterenol in asthma management in terms of their binding sites?
An antlanxlety medication, clorazepate, can bind to several receptors. These receptors differ In the amino acıd AA positlioned near the carboxyl group of clorazepate. All chemical groups are lonized according to pH 7. Which of the receptors is likely to have the highest binding energy with clorazepate? Phe sidechain - AA o-H Tyr Phe A. AA - Ser B. AA - Asp C. AA - Glu D. AA - Arg E. AA - Gly
In one type of hemoglobin mutant the amino acid change generates a strong ionic interaction stabilizing the T state conformation, but only under conditions of lower pH, e.g., at pH 7.2 compared to pH 7.6. Explain what effect this mutation would have on the amount of O2 delivered to the tissue. More O2 delivered to the tissue because the R-T equilibrium would be shifted to the T state in tissues. More O₂ delivered to the tissue because the R-T equilibrium would be shifted to the T state in lungs. Less O2 delivered to the tissue because the R-T equilibrium would be shifted to the T state in lungs. Less O₂ delivered to the tissue because the R-T equilibrium would be shifted to the T state in tissues. More O2 delivered to the tissue because the R-T equilibrium would be shifted to the R state in tissues.
-Inhibitor +Inhibitor [S] (mM) Vη&νβσπ: (μmol/sec). ν0&νβσπ;&νβσπ:(μmol/sec) 0.0001 33 17 0.0005 71 50 0.001 83 67 0.005 96 91 0.01 98 95 What is the TYPE of iinhibitor?