8. In a patient with anemia, the presence of Heinz bodics in the RBCS was theresult of the hemoglobin subunits aggregation due to the oxidation of -SHgroups of Hb cysteine residues with active oxygen forms and the formation ofdisulfide bonds. What metabolic disorders in the RBC can be the cause of thisclinical case? To solve the problem:a) indicate which reactions maintain cysteine residues in a reduced state;b) name the coenzyme involved in this process, write a diagram of the process inwhich the reduced form of this coenzyme is formed;c) indicate the enzyme which deficiency may lcad to a lack of the reducedcocnzyme and be the cause of the clinical case described above.

Answered: Image /qna-images/answer/c83ddc10-a538-4da9-b7cb-5ee61ec8f54c.jpg

Answered: 8. In a patient with anemia, the…

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 20P: Understanding the Mechanism of Hemolytic Anemia Genetic defects in glycolytic enzymes can have...

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In an experiment, hemoglobin is dissociated in a buffer and a subunit is isolated to study for its oxygen binding affinity. (i) What is the shape of the oxygen dissociation curve is expected in the experiment?Explain why. (ii) Is the Km of the isolated subunit higher or lower than the Km of an intact hemoglobin?
2. It is known hemoglobinopathies, whi ch arise due to mutations in one of histidines a- or B- chains binding with the iron in the heme gro up.These mutations stabilize the iron in Fes form. Some drugs (eg. sulfonamides) or chemicals( eg.anilin) also can cause methemoglobinemia. Suggest, how change the properties of Hb in these cas es. For this:1)Describe the structure and function of Hb A as a transport protein. 2) Explain the role ofiron ions in act ive centers of Hb for the binding of O23) How many molecules of Oz can bind mutant Hb, if mutation occurs in a- subunits? 4) Why can ascorbic acid be used to tr eat of such patients.
1. What are two features of Viperin-like enzyme structure that make it different OR similar to haemoglobin? 2. Based on the structural properties of Viperin-like enzyme, how resistant (or sensitive) would your Viperin-like enzyme be to heat denaturation and why?
What qualitative effect would you expect each of the following to have onthe P50 of hemoglobin?(a) Increase in pH from 7.2 to 7.4(b) Increase in PCO2 from 20 to 40 mm Hg(c) Dissociation into monomer polypeptide chains(d) Decrease in 2,3-BPG concentration from 7 mM to 5 mM in red cells.
9. If 32p-labeled inorganic phosphate were introduced to erythrocytes undergoing glycolysis which of the following molecules would you NOT expect to detect 32p in? ** Multiple answers: Multiple answers are accepted for this question a. Fructose 1-6 bisphosphate b. 3-Phosphoglyceraldehyde c. Dihydroxyacetone phosphate d. 2-Phosphoglycerate e. 1-3 bisphosphoglycerate f. Phosphoenolpyruvate g. 3-Phosphoglycerate h. Pyruvate i. Glucose 6-Phosphate
In oxygenated hemoglobin, pKa 5 6.6 forthe histidines at position 146 on the -chain. In deoxygenated hemoglobin, the pKa of these residues is 8.2. How can this piece ofinformation be correlated with the Bohr effect?
14 carbon methyl pyruvate is added to isolated liver tissue and molecule is used to block succinate dehydrogenase completely. After sometime isocitrate is formed to carry label in carbon 2 and 4 explain how can this happen ?
hi there you have said Microcytic anemia could be caused due to both iron deficiency anemia and thalassemia. could you expalin in detail why and how. With the a of diagram Along with mechanims.
3. When muscles are more active physiological conditions change to affect oxygen binding to Hemoglobin. Briefly describe the changes that occur and why this affects hemoglobin function. Draw the shifted curve on the graph above. A. What physiological conditions change during exercise (levels of what molecules are increasing/decreasing)? B. How do these molecules directly affect Hb’s structure ? What interactions does this stabilize ? C. How do these interactions affect the affinity of Hb for O2? How would this affect the binding curve for Hb? Draw on the graph provided. D. How will this shift in the binding curve affect the function of Hemoglobin ? E.Where does the physiological pO2 in the tissues fall on the O2 binding curve ? In the lungs ? Why is this physiologically important?
Apohemoglobin (apoHb) is a dimeric globular protein with two vacant heme‐binding. The preparationof apoHb is based on partial hemoglobin (Hb) unfolding to facilitate heme extraction into an organic solvent. What is an appropriate method for removing the heme? a. An acidic buffer to protonate the His axial ligand in the presence of ureaas the denaturing agent. b. An acidic buffer to protonate the His axial ligand in the presence of mercatoethanol as the denaturing agent. c. A basic buffer to deprotonate the His axial ligand in the presence of ureaas the denaturing agent. d. An basic buffer to protonate the His axial ligand in the presence of mercatoethanol as the denaturing agent.
"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?
2. One manifestation of cytochrome oxidase deficiency in humans is severe muscle weakness. Briefly explain why. 3. Clostridium bacteria are killed in the presence of molecular oxygen. Would you expect Clostridium to produce catalase? Briefly explain.

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