How does the altered primary structure of hemoglobin from sickle cell patients (hemoglobin S)...
Question:
How does the altered primary structure of hemoglobin from sickle cell patients (hemoglobin S) affect its tertiary structure?
Sickle Cell Anemia:
Sickle cell anemia is a disorder that appears when a sufficient number of RBCs (red blood cells) are not present in an individual's blood. In sickle cell disease, red blood cells' shape has changed into a sickle shape. The change in the form of RBCs makes them rigid that disrupts their flow inside the blood vessels.
Answer and Explanation: 1
Become a Study.com member to unlock this answer! Create your account
View this answerSickle-shaped red blood cells stick together, and this can cause a blockage inside the blood vessels. Due to blockage, severe complications can appear...
See full answer below.
Ask a question
Our experts can answer your tough homework and study questions.
Ask a question Ask a questionSearch Answers
Learn more about this topic:
from
Chapter 5 / Lesson 17What is heme? Learn the definition of heme and about the molecule's structure. Also, read about the heme group in hemoglobin and what hemoglobin is made of.
Related to this Question
- When people have sickle cell anemia, they cannot efficiently transport oxygen. What are the implications at the cellular level (hint: why do cells need oxygen)? Describe how this deprivation of oxygen might make these patients feel. Why doesn't a blood tr
- Why are normal erythrocyte and hemoglobin levels important in blood?
- Describe the pathophysiology that contributes to low hemoglobin and hematocrit in a hemodialysis patient.
- Why does hemoglobin bind so much more readily to a second and third oxygen molecule than to the first?
- Discuss the role of hemoglobin in the transport of O_2 and CO_2. What factors affect the affinity of hemoglobin for O_2?
- What affect might you expect the precipitation of hemoglobin S and the subsequent cell sickling to have on oxygen delivery in an individual with sickle cell disease?
- (a) Why do the red blood cells of persons with sickle cell disease tend to form blood clots? (b) What are the consequences of this clotting tendency?
- Why is the pharmacological reactivation of fetal hemoglobin in a patient with sickle cell anemia often a successful treatment? a. Fetal hemoglobin is better able to release carbon dioxide than is adult hemoglobin. b. Fetal hemoglobin binds more oxygen mol
- The carbamino effect describes a change in the conformation of hemoglobin that is induced by a(n) ____?
- Fetal hemoglobin binds 2,3-BPG with a lower affinity than adult hemoglobin. Will the O2 saturation curve for fetal hemoglobin be shifted to the right or to the left from the curve for adult hemoglobin? Briefly explain your answers.
- How does sickle cell anemia cause the vaso-occlusive crisis?
- Fetal hemoglobin binds 2,3-BPG with a lower affinity than adult hemoglobin. Will fetal hemoglobin have a higher or lower affinity for O2 than the mother's hemoglobin? Briefly explain your answer.
- Explain how anemia, polycythemia, low erythropoietin levels, splenectomy, and infection affect blood flow.
- Changes in the hematocrit affect the movement of blood through the body. Describe how increases and decreases in the hematocrit affect the function of the heart and the ability to transport oxygen to the tissues.
- Fetal hemoglobin binds 2,3-BPG with a lower affinity than adult hemoglobin. Will fetal hemoglobin have more or less 2,3-BPG bound than the mother's hemoglobin? Briefly explain your answer.
- Hyperventilation leads to decreased arterial PCO2. How will this affect O2 binding to hemoglobin at the lungs and at the tissues?
- Does the hematocrit increase or decrease if you have Sickle cell anemia?
- Predict the cellular adaptations erythrocytes undergo when chronic hypoxia is present. How would this be evident on an oxygen-hemoglobin dissociation curve?
- Why do the following factors cause sickling of the red blood cells in a child with hemoglobin S (HbS): a) Decreased oxygen in the blood (pO2) b) Decreased pH c) Dehydration
- Why is the protein hemoglobin necessary for successful circulation of oxygen?
- Portion of hemoglobin molecule that binds O2 - Fe2+ - ferritin - globin - heme - transferrin
- During hyperventilation too much carbon dioxide leaves the lungs. What effect will this have on the function of hemoglobin? Will the hemoglobin deliver more or less oxygen to the tissues? Explain your answer.
- Compare maternal and fetal hemoglobin in their primary, secondary, tertiary, and quaternary structures.
- Explain the role of hemoglobin in the circulatory system. How carbon monoxide poisoning occurs?
- If a red blood cell is affected by sickle cell disease, which of the following is true? A. Abnormal hemoglobin causes abnormal structure of the red blood cell. B. The plasma membrane of the red blood cell allows too much fluid into the cell because of a h
- The reaction of hemoglobin and oxygen is complicated. Explain some of this relationship in regards to the Hb-O2 saturation curves and why breathing at altitude is more difficult and CO2's role. (mention affinity for O2/CO2 and factors affecting the right
- Compare fetal hemoglobin binding O_2 to maternal hemoglobin binding of O_2. Why is this important?
- How does fetal hemoglobin enhance oxygen transfer across the placenta (from mother to baby)?
- Describe the picket fence porphyrin models for hemoglobin, and show how they helped elucidate the mode of binding of dioxygen to hemoglobin.
- What are B-Hemoglobin, S-B-Hemoglobin, and d-hemoglobin?
- 1. What is the function of each of these reactions in a person's body? a) Clotting serves to: b) Agglutination is a reaction to: 2. Why are both hematocrit and hemoglobin content performed as sepa
- As a doctor, you find a patient that does not have hemoglobin. Explain why you could not treat this patient with an infusion of myoglobin.
- How is the dissociation of O2 from hemoglobin affected when you exercise? Describe: 1) the two relevant physiological changes 2) the reasons behind those two changes 3) the effect on O2 dissociation
- What is pathophysiology of sickle cell anaemia?
- The reaction of hemoglobin and oxygen is complicated. Explain some of this relationship, in regards to the Hb-O2 saturation curves, and why breathing at altitude is more difficult, and CO2's role. (me
- The affinity of hemoglobin for oxygen changes with pH. What is affecting the pH of the blood? a. The blood changes its pH based on the amount of carbon dioxide dissolved. b. The blood changes its pH based on the amount of oxygen dissolved. c. The pH of th
- 1) What is the Renin-angiotensin pathway(RAA Pathway)? 2) Explain what the hemoglobin disassociation curve is in detail.
- What factors cause hemoglobin to unload more oxygen as blood flows through capillaries of metabolically active tissues, such as skeletal muscle during exercise?
- What is the name of the condition which could produce a higher-than-normal hemoglobin content and give a physiological reason? Why would this occur?
- Describe how the CO2 molecule is transferred from the RBC to the alveolus
- Mature erythrocytes release their O2 at actively metabolizing tissues due to lowered pH and O2 levels. Why? What other factors might cause hemoglobin to release O2? How might a drop in pH cause hemoglobin to release O2?
- What is the relationship between hemoglobin and P_{O_2}?
- What does it take to bind oxygen to the heme in either myoglobin or hemoglobin?
- Does adult or fetal hemoglobin have a higher affinity for O2? What is the significance of this?
- What is the most important factor that determines how much O2 binds to hemoglobin? Define and describe key terms: fully saturated,partially saturated, and percent saturation of hemoglobin.
- Explain the relationship between hemoglobin and the partial pressure of oxygen as described by the oxygen-hemoglobin dissociation curve within homeostatic conditions. In addition, describe the effects of a change in temperature (Haldane effect), pH (Bohr
- How do we refer to hemoglobin when it carries oxygen or carbon dioxide? Is it acting as a weak acid or a weak base?
- How is the production of red blood cells regulated to maintain homeostasis of the oxygen-carrying capacity of blood?
- Explain the flow of a hemoglobin molecule from the lung capillaries to the heart, to the kidney, and back to the lungs again, mentioning the names of the major blood vessels and the movement of blood through the chamber of the heart.
- Would a deficiency in hemoglobin be more detrimental to oxygen transport or carbon dioxide transport? Explain.
- How is the platelet plug altered with primary immune thrombocytopenic purpura, heparin-induced thrombocytopenia, and Plavix?
- The main role of the protein hemoglobin is to transport oxygen. Red blood cells use hemoglobin to pick up oxygen from the lungs and then drop it off at subsequent cells. Blood also carries sugar (glucose) around the body. Glucose is picked up in the intes
- Which are true of red cell changes in the older adult? a. During a stressful situation such as hemorrhage, the red blood cells of the elderly are not replaced as quickly as a younger adult. b. The elderly are able to maintain hemoglobin and hematocrit lev
- In thalassemia, a type of anemia, the hemoglobin molecule is malformed. The malformation prevents hemoglobin from carrying and delivering the correct amount of oxygen to the cells. Which important physiological concept does this example illustrate?
- Compare the structures of hemoglobin and myoglobin.
- A molecule of hemoglobin carries four heme groups, ringed shaped molecules each with a single central iron atom. By binding reversibly to oxygen gas through its iron atom, heme enables to pick up oxygen in the lungs and release it in the tissue. How is th
- Explain how hyperventilation and hypoventilation alter levels of carbon dioxide in the blood.
- What type of hemoglobin is found in fetal and adult RBCs?
- Mature erythrocytes release their O2 at actively metabolizing tissues due to lowered pH and O2 levels. 1. Why? 2. What other factors might cause hemoglobin to release O2. 3. How might a drop in pH
- How does an increased level of LDL relate to the development and progression of atherosclerosis?
- What is the difference between hemoglobin and bilirubin?
- 1. Mature erythrocytes release their O2 at actively metabolizing tissues due to lower pH and O2 levels. Why? 2. What other factors cause hemoglobin to release O2?
- Hemoglobin is converted to in all of the body systems except the respiratory system. a. carbiminohemogobin b. oxyhemoglobin c. deoxyhemoglobin d. monoxidehemaglobin
- Explain how blood flow to an alveolar area is altered to match airflow to that area.
- When oxygen is loaded onto hemoglobin in the lungs, hemoglobin is called _______ and when oxygen is unloaded from the hemoglobin at the tissues it is called _______..
- No oxygen-carrying blood substitute is currently available. However, researchers are experimenting with compounds that function like hemoglobin. What properties would make a synthetic compound a potential hemoglobin substitute?
- Is the p50 higher or lower than normal in (a) hemoglobin Yakima (b) hemoglobin Kansas (c) hemoglobin Rainier? Briefly explain.
- Explain the hemoglobin A 1 C level for an individual without diabetes.
- What is the difference between fetal and adult hemoglobin?
- When Pco2 is increased in the blood, hemoglobin will do which of the following? a. Release oxygen b. Bind more oxygen c. There is no effect on oxygen
- What does hemoglobin have a stronger affinity to than oxygen?
- Hemoglobin is a protein which binds oxygen in the lungs and releases it in the capillaries. Interestingly, your body controls this intake and drop off of oxygen by having different pH's at the two locations. (a) Explain how oxygen binds to heme (and if a
- Why does myoglobin store oxygen and hemoglobin transport oxygen?
- The oxygen binding site in hemoglobin and myoglobin is called: a) BPG b) heme c) proximal-His d) N-terminal carbamate
- When RBCs are eaten by phagocytes in the liver, the hemoglobin is broken down. a. What happens to the iron? b. What happens to the globin (protein)? c. What happens to the heme?
- The hemoglobin levels measure 15 g/d. What is the estimated value of the hematocrit? A. 45% B. 55% C. 65% D. 35%
- What are the dietary factors affecting red blood cell production? Explain your answer.
- A molecule of hemoglobin that is 100% saturated would have oxygen molecules.
- Will O2 passively diffuse and bind with hemoglobin that is less than 1 mm from the surface of a blood sample?
- Describe the changes in clotting and bleeding balance during disseminated intravascular coagulation (DIC). What are the most important blood coagulation tests used to monitor the patients receiving heparin and warfarin?
- How might the removal of the spleen result in an increase in the number of circulating platelets?
- What is haemoglobin F? Why does the fetus need a different type of haemoglobin?
- (a) What is hemoglobin? (b) What inorganic element is fundamental in the composition of hemoglobin?
- Fill in the blanks. Hemoglobin not bound with oxygen is called _________ or __________.
- Explain the reason for transfusion reactions resulting from the administration of mismatched blood.
- Why is it important to know what blood type antigen is on red blood cells when someone receives blood after a surgery? (use carbohydrate-related terms)
- Which of the following influences both hemoglobin and myoglobin activity adversely? a. Amino acids. b. Oxygen. c. Protons. d. Carbon monoxide.
- Which process is most responsible for the sickling of cells seen in sickle cell disease? a) aggregation of the oxygenated R form of hemoglobin-S to form insoluble fibers b) aggregation of the deoxygenated T form of hemoglobin-S to form insoluble fibers c)
- Why doesn't a transfusion reaction occur the first time an Rh-negative patient is exposed to Rh-positive blood?
- A) Which part of the hemoglobin molecule does the oxygen bind to? Select one: a. globulin b. heme disc c. iron d. alpha chain e. beta chain B)The stomach contains 3 layers of skeletal muscle. Select one: a.True b.False
- How would carbon monoxide poisoning affect a person's coloring, particularly of the mucous membranes? How would it affect the hemoglobin concentration, hematocrit, and percent oxyhemoglobin saturation? How would chronic carbon monoxide poisoning affect th
- How does beta-adrenergic receptor activation lead to increased myocardial contractility?
- Effect of exercise on tissue PO_2: With a decrease of 20 mmHg in the tissues, will the saturation of hemoglobin decrease significantly? How does this help the tissues?
- Explain why it would not be possible to accurately measure hemoglobin concentration if the RBCs were not first lysed. Leukemia is a type of bone marrow cancer in which the hematopoietic tissue produce
- Haemoglobin also spelled hemoglobin and abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein in the red blood cells of all vertebrates as well as the tissues of some invertebrates. What is its function?
- If your blood glucose is too high, what is the effector and effect?
- How would hemoglobin content differ in a person living in Philadelphia (elevation: 39 feet) as compared to someone living in Denver (elevation: 5,280 feet). Why?
- How would the hemoglobin content differ in person living in Philadelphia (elevation 39 feet) compared to someone living in Denver (elevation 5280 feet)? Why?
- How would the hemoglobin content differ in a person living in Philadelphia (Elevation: 39 feet) compared to someone living in Denver (Elevation: 5280 feet)? Why?
- What is hemoglobin referred to when it carries oxygen or carbon dioxide? Is it acting as a weak acid or a weak base?