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    Hemoglobin

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    BIOCHEMISTRY: Protein Function–Myoglobin and Hemoglobin by A. Scheider 1 Tuesday‚ March 12‚ 13 Alpha helix polypeptide chains Heme complex with Oxygen attached to iron Heme complex without Oxygen attached to iron Beta sheet polypeptide chains Model of Hemoglobin Molecule 2 Tuesday‚ March 12‚ 13 Hemoglobin: quick facts Hemoglobin is a protein that carries Oxygen and releases Oxygen to the body via the blood circulation. Hemoglobin is made of 4 polypeptide chains with each chain

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    Hemoglobin

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    1. State the principle of the test (the general laws or facts of nature underlying the working of a device or test) Hemoglobin which is also known as HbG or Hb is composed of 2 alpha and 2 beta chains. They both transport a heme molecule. HbG is the primary constituent of red blood cell cytoplasm and transports oxygen from the lungs to the tissues and then returns carbon dioxide to the lungs. HbG can be used to diagnose or monitor a number of conditions. Anemia is one of those conditions.

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    Hemoglobin Model

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    Biochemistry 208.5.3: Protein Function: Myoglobin and Hemoglobin Hemoglobin model: note the 02 being carried by molecule. Pipe cleaners=subunits Green marsh mellow=iron molecule Yellow marsh mellow=oxygen molecule Orange cards= heme groups (wolfe‚ 2000) Oxygenated/deoxygenated oxygenated • 02 bound • Bright red • Subunit is in relaxed form • Higher affinity for 02 • Affinity for oxygen is cooperative‚ which means that the affinity for 02 increases with each bound molecule

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    Plant Hemoglobin

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    Plant Hemoglobin Hemoglobin is a protein-iron compound found within the red blood cells of most vertebrates and is responsible for the cell’s red pigment. These red blood cells carries oxygen from the lungs to the rest of the tissue cells throughout the rest of the body. Just as hemoglobin transports oxygen in humans‚ they have also been found transporting oxygen within plants. In plants‚ there are two types of hemoglobin that can be found; symbiotic and non symbiotic. Oxygen is used

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    HEMOGLOBIN AND MYOGLOBIN

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    HEMOGLOBIN AND MYOGLOBIN I. OXYGEN CARRIERS A. Why do we need oxygen carriers? i. Cannot carry enough in blood to meet metabolic demand ii. Oxygen is very reactive – oxidizes iii. Oxygen cannot diffuse very easily (we have thick skin) B. Properties of a good oxygen carrier i. Binds oxygen at a high [O2] ii. Doesn’t oxidize cellular components iii. Gives up oxygen on demand C. Hemoglobin and Myoglobin i. Cooperativity 1. Hemoglobin needs to have high affinity to bind O2 in the lungs‚ but low affinity

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    Definition of Hemoglobin • Description of Hemoglobin • Questions To Ask Your Doctor About Hemoglobin Definition of Hemoglobin Hemoglobin is the iron-carrying protein found in red blood cells that binds to oxygen. Description of Hemoglobin Hemoglobin is a crystallizable‚ conjugated protein consisting of an iron-containing pigment (called heme or hematin) and a simple protein‚ globin. In the lungs‚ it combines readily with oxygen to form a loose‚ unstable compound called oxyhemoglobin

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    Hemoglobin In Ice Fish

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    blood is almost transparent because of the lack of red blood cells‚ and they are the only vertebrate that does not have circulating hemoglobin. Those organisms are referred to as Ice fish‚ and they are one of the unique organism that live in Southern Ocean around Antarctica and Southern South America‚ where water temperatures remain relatively stable. Hemoglobin is a protein within mammalian red blood cells that transports oxygen for delivery to tissues throughout the body. Having red blood cells

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    Hemoglobin Research Paper

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    PROTEIN FUNCTION MYOGLOBIN AND HEMOGLOBIN HEMOGLOBIN Key: 4 subunits – fuzzy sticks; blue‚ yellow‚ red‚ and brown 4 heme groups – red‚ white‚ and blue twizzler 4 iron atoms – chocolate Rollo candies 4 oxygen molecules bound to the iron – red twizzler in a circle (Hudson-Miller‚ Hemoglobin‚ 2013). MAJOR DIFFERENCES BETWEEN OXYGENATED AND DEOXYGENATED STATES OF HEMOGLOBIN Oxygenated State of Hemoglobin Deoxyenated State of hemoglobin One hemoglobin can carry 4 oxygen Not bound to oxygen Plantar

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    Principles of Life Hillis • Sadava • Heller • Price Test Bank Chapter 37: Gas Exchange in Animals TEST BANK QUESTIONS (By Paul Nolan) Multiple Choice 1. If you were atop Mt. Everest‚ how many cubic meters of air would you need to breathe in order to gain the same number of oxygen molecules that you would gain from one cubic meter of air at sea level? a. 2 b. 3 c. 5 d. 9 e. 10 Answer: b Textbook Reference: 37.0 Introduction Page: 729 Bloom’s Category: 3. Applying 2.

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    figure out the possible ways to prevent ourselves form Thalassemia (الرؤوف‚ 2009).Third reasons is the treatment of Thalassemia. WHAT IS THALASSEMIA? Thalassemia is genetic disorders that involve the decreased and defective production of hemoglobin‚ a molecule found inside all red blood cells (RBCs) that transports oxygen throughout the body (Miller‚ Thalassemias‚ 2008). As (Hashemi‚ 2011) says "Thalassemia is blood disorders ". As (Clinaero‚ n.d.) says" There are mild and severe forms of

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    is a group of inherited red blood cell disorders. People with Sickle Cell Disease have abnormal hemoglobin‚ called hemoglobin S or sickle hemoglobin‚ in their red blood cells. People with SCD inherit two abnormal hemoglobin genes‚ one from each of their parents. One of these abnormal hemoglobin genes causes the production of hemoglobin S in the body.1 When a person has two hemoglobin S genes‚ Hemoglobin SS‚ this disease is called Sickle Cell Anemia.1 This is the most common and most severe case of

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    Hemoglobin Research Paper

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    though adult hemoglobin‚ Hb A‚ can easily release its oxygen due to the low saturation in the vein‚ normally at that level of oxygen‚ hemoglobin cannot bind oxygen to itself. In the ordinary course of things‚ fetus would not be able to bind the required oxygen for its circulation from the maternal circulation‚ but to overcome this problem fetus produces another variant of hemoglobin called Fetal hemoglobin‚ Hb F. This type of hemoglobin has a higher affinity compared to adult hemoglobin‚ that can achieve

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    first suggestion that genes might provide the information for all proteins came from Linus Pauling’s lab at Caltech. He and his student Harvey Itano studied hemoglobin‚ the protein in red blood cells that transports oxygen from the lung to metabolically active tissues‚ like muscle‚ where it is needed. In particular‚ they focused on the hemoglobin of people with sickle-cell disease‚ also known as sickle-cell anemia‚ a genetic disorder common in Africans‚ and therefore among African Americans as well

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    abnormality in the oxygen-carrying protein hemoglobin found in red blood cells. This leads to a propensity for the cells to assume an abnormal‚ rigid‚ sickle-like shape under certain circumstances. Sickle-cell disease is associated with a number of acute and chronic health problems‚ such as severe infections‚ attacks of severe pain‚ stroke‚ and an increased risk of death. Sickle-cell disease occurs when a person inherits two abnormal copies of the hemoglobin gene‚ one from each parent. Several subtypes

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    Question 1 (4 marks)- Compare and contrast the structures of myoglobin and hemoglobin. How does each structure relate to its function? Myoglobin and haemoglobin‚ are both globular proteins‚ however‚ myoglobin is present in the heart and skeletal muscles‚ while haemoglobin is only found in red blood cells. The function of myoglobin is to bind and release oxygen to the muscle cells‚ whereas the function of hemoglobin is to transport oxygen from the lungs to the tissues‚ and transport carbon dioxide

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    Sickle-Cell Anemia is a genetic blood disorder caused by the presence of an abnormal form of hemoglobin. These hemoglobin molecules tend to aggregate after unloading oxygen forming long‚ rod-like structures that force the red cells to assume a sickle shape. Unlike normal red cells‚ which are usually smooth and malleable‚ the sickle red cells cannot squeeze through small blood vessels. When the sickle cells block small blood vessels‚ the organs are deprived of blood and oxygen. This leads to periodic

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    Thalassemia Disorders

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    youngest son. I am fortunate and very grateful for the diagnosis at age eleven. I now can ensure that youngest son will go on to raising his very own happy healthy children. Thalassemia is a group of related blood disorders that cause abnormal hemoglobin production. It is a genetic disorder that is recessive; therefore both parents must be carriers to pass on the disorder in its major form. Thalassemia is categorized into two types‚ major and minor. Individuals suffering from the major form‚ tend

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    Sickle Cell Anemia

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    process is known as sickling. What is Sickle Cell Anemia? It is a blood disorder that affects hemoglobin‚ red blood cells with normal hemoglobin move easily through the bloodstream‚ delivering oxygen to all of the cells of the body. Normal red blood cells are shaped like doughnuts with the centers partially scooped out and are soft and flexible. Sickle cell anemia occurs when an abnormal form of hemoglobin is produced. HbS molecules tend to clump together‚ making red blood cells sticky‚ stiff‚ and

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    Sickle Cell Anemia

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    because of a mutation in the hemoglobin gene. Sickle cells are stiff and sticky. They tend to block blood flow in the blood vessels of the limbs and organs. Blocked blood flow can cause pain‚ serious infections‚ and organ damage. Life expectancy in people who have this disease is shortened.  Anemia is a condition in which your blood has a lower than normal number of red blood cells. This condition also can occur if your red blood cells don’t contain enough hemoglobin. Red blood cells are made in

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    Sickle cell anemia (SCA) is a genetic disorder that is hereditary. It affects the blood‚ and is caused when the hemoglobin in blood cells are deprived in oxygen from the proteins. These cause normal round blood cells‚ to have are rigid sickle shape. People affected by SCA have a higher risk of death‚ stroke‚ severe attacks‚ and severe rushes of pain. James Herrick discovered an anemia‚ and found bizarre sickle-shaped cells in 1910. A treatment for the disease was discovered in the 1920s by E. Vernon

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