Some of the reactions of NO in the blood do not cause problems at low concentrations but can upset the normal reactions of hemoglobin if there is a large concentration of NO. The same reactions can cause trouble if a synthetic blood substitute contains a molecule similar to hemoglobin but does not contain all the other enzymes normally contained in red blood cells. Explain what this problem is and how it arises.

Some of the reactions of NO in the blood do not cause problems at low concentrations but can upset the normal reactions of hemoglobin if there is a large concentration of NO. The same reactions can cause trouble if a synthetic blood substitute contains a molecule similar to hemoglobin but does not contain all the other enzymes normally contained in red blood cells. Explain what this problem is and how it arises.

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 3P: Effects of Changing Metabolite Concentrations on Glycolysis In an erythrocyte undergoing glycolysis...

See similar textbooks

Similar questions

Comparison of Fetal and Maternal Hemoglobins.Studies of oxygen transport in pregnant mammals show that the O2-saturation curves of fetal and maternal blood are markedly different when measured under the same conditions. Fetal erythrocytes contain a structural variant of hemoglobin, HbF, consisting oftwo a and two g subunits (α2γ2), whereas maternal erythrocytes contain HbA (α2β2). a)Which hemoglobin has a higher affinity for oxygen under physiological conditions, HbA or HbF? Explain. b)What is the physiological significance of the different O2 affinities? c)When all the BPG is carefully removed from samples of HbA and HbF, the measured O2-saturation curves (and consequently the O2affinities) are displaced to the left. However, HbA now has a greater affinity for oxygen than does HbF. When BPG is reintroduced, the O2-saturation curves return to normal, as shown in the graph. What is the effect of BPG on the O2affinity of hemoglobin? How can the above information be used…
You happen to pass a bar. Distracted by your entrance into the bar, one of the humans inadvertently drank a beverage containing 80 ml methanol. Unfortunately, no medical personnel are on the station, and you do not have access to sickbay. Assume that methanol and ethanol have densities of 0.79 g/ml, and that the alcohols distribute themselves rapidly over the total volume of 73 liters of body fluids of your host. A quick check of the biochemistry textbook that you always carry with you when traversing the promenade reveals that the Km of alcohol dehydrogenase for ethanol is 1 mM and for methanol the Km is 10 mM, and reminds you that alcohol dehydrogenase converts ethanol into acetaldehyde (which can then be converted to acetyl-CoA). Alcohol dehydrogenase also converts methanol into formaldehyde, which is quite toxic to humans. Ingesting 80 ml of methanol will permanently harm the human unless you intervene.b. Someone has a single 600 ml bottle of Romulan ale (52% ethanol), which he is…
Bohr for me, not for thee. Does myoglobin exhibit a Bohr effect? Why or why not?
Some terms will not be used. The prosthetic group of hemoglobin and myoglobin is The organic ring component of heme is Under normal conditions, the central atom of heme is In the central iron atom is displaced 0.4 Å out of the plane of the porphyrin ring system. The central atom has bonds: to nitrogen atoms in the porphyrin, one to a residue, and one to oxygen. Answer Bank Fe3+ three heme serine deoxyhemoglobin four Fe2+ oxyhemoglobin рoгphyrin histidine six cysteine
Animals breathe in oxygen. What is this atmospheric oxygen used for in the human body? (Give the name of the process where atmospheric oxygen is used and explain what happens to the atmospheric oxygen molecule.)
"Hemoglobin can be in either an oxy- or deoxy- state at a given pH. Given the appropriate pKa values, calculate fraction protonated at a given pH" How would I do this?
(No more than one page). Explain why quaternary structure is necessary for cooperativity and allosteric regulation. Use hemoglobin as an example. Include the various allosteric effectors that influence oxygen binding.
in human 2. Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout. several medications are used to inhibit the activity of xanthine oxidase and reduce the production of uric acid. You are a biochemist and just discovered a chemical that can inhibit the activity of the human xanthine oxidase. When analyzing its mode of inhibition, you found that the enzyme inhibitor complex requires 450 kJ.mol to dissociate and that it displays kinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministry of health for approval as a medication for gout. Based on the data provided, are they going to authorize it as a medication or not? Explain?
Mechanisms of catalysis: 2.6 Mechanism of lysozyme summary. These mechanisms involve several of the above-mentioned catalyses. In these summaries, do not just draw a diagram of the proposed mechanisms. It is more important to understand which reaction steps involve what kind of catalysis and how these help to reduce the activation energy needed for the reaction (e.g. a step in the reaction mechanism could be electrostatic catalysis to stabilise the transitions state)
Metabolic regulation (Ch. 15) 1. The Vmax of the enzyme glycogen phosphorylase from skeletal muscle is much greater than the Vmax of the same enzyme from liver tissue. (a) What is the physiological function of glycogen phosphorylase in skeletal muscle? In liver tissue? (b) Why does the Vmax of the muscle enzyme need to be larger than that of the liver enzyme?
Why brain, eyes and RBCS cannot use fatty acids? Explain.
Please ASA. Thanku. In the reaction Na + Cl à Na+ + Cl-, which component is said to become ‘oxidized’ and which is considered reduced? Na, Cl Cl, Cl Na, Na Cl, Na