...Having reviewed the food journal analyses and evaluated personal activity balance I have reached several critical conclusions. First important thing that I have learned about myself is the fact that I tend to consume products insufficient to number of servings. Thus, regardless of my genuine attempts to eat products of all major food pyramid categories, such as grains (food made of wheat, rice, oats, cornmeal, cereal grains), vegetables (dark green, orange, starchy, dry beans and peas, other), fruits (berries, melons, bananas, apples, etc.), dairy products (milk, cheese products, yogurts, milk-based deserts) and meat and beans (meats, poultry, eggs, fish, nuts and seeds ), my daily intake usually remains inadequate. After giving it more thought I have realized that the reason for this is my tendency to divide the categories of pyramid among several intakes. For example, after having eaten something from the vegetable or fruits group I do not consider adding another serving of those to my remaining meals. Some of the product groups, such as, for example, meat, I have been purposefully limiting, aware of it being very rich in fat and hard to digest. This situation is even more complicated by the fact that my choice of products is frequently monotonous, thus, leading to the inadequate daily supply of the listed food groups. Moreover, while undersupplying myself with most categories, I simultaneously tend to have a rather high intake of protein because of my weak understanding of...
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...Protein Function Biochemistry Task #3 Diane Pruchnicki Student ID# 000472055 Oxygenated vs. Deoxygenated Hemoglobin OXYGENATED HEMOGLOBIN • Heme shape is flattened or planar, due to oxygen tugging on iron • Hemoglobin can better bind with oxygen, known as R-state, or relaxed state • Iron can easily picks up oxygen • Hemoglobin reaches the lungs and an oxygen molecule adheres to the iron • Blood is bright red in color, due to oxygenated blood traveling from heart to systemic circulation DEOXYGENATED HEMOGLOBIN • Heme shape is pyramid/dome shaped • Hemoglobin binding without oxygen, known as a T-state, or tense state • T-state makes oxygen binding more difficult • Blood is maroon/blue in color, due to decreased amount of oxygen. Blood is traveling back to heart from systemic circulation pH Impact on Binding & Release of Oxygen by Hemoglobin Comparison between Hemoglobin and Myoglobin Structure Hemoglobin Diseased Cells Difference from Normal RBC’s in Oxygen Transportation • Normal RBC’s keep a disc-like shape (doughnut shape minus the hole), while moving easily through the small arteries and capillaries, where they release oxygen to the peripheral tissues. These normal RBC’s carry oxygen from the lungs to the rest of the body without difficulty. • Sickle cells are known to be sticky/stiff and form into a sickle, or crescent, shape when they lose oxygen. With the loss of oxygen, these...
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...to eat ice and her tongue was sore. She sought an appointment with her physician and throughout her exam they find that she has tachycardia (an abnormally rapid heart rate), pale gums and nail beds, and her tongue is swollen. Her physician diagnosed her with anemia due to iron deficiency and an oral iron supplement was prescribed. Below are some questions with the explanation of why this might have happened. 1. Describe the structure of a molecule of hemoglobin and explain the role played by iron in the transport of oxygen. Found in red blood cells, hemoglobin is a protein that carries oxygen molecules and carbon dioxide molecules throughout the body and are responsible for making the red blood cells red. Made up of red heme pigment bound the protein globin it makes up the hemoglobin. Hemoglobin consists of four subunits, two alpha and two beta polypeptide chains and a non-protein heme group, which is an assembly of cyclic ring structures surrounding an iron ion that is surrounded by a nitrogen atom. A hemoglobin molecule can transport four molecules of oxygen because each iron atom can combine reversibly with one molecule of oxygen. Leading to a change in oxidation state for iron from +2 to +3 the iron atom of each heme group can bind to diatomic oxygen. It delivers oxygen easily when it exhibits a relaxed state that will release the oxygen and it will reduce the iron atoms from +3 to +2. It becomes easier for oxygen to increase when more oxygen bind to the heme...
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...descendants spread around the world. For instance, in United States one in 400 African-American infants is born with sickle cell disease annually (Ibid). Description of Sickle Cell Disease Sickle cell disease comprises of red blood cell disorders whose main feature is abnormal hemoglobin in the red blood cells. Hemoglobin is an oxygen carrying protein in the red blood cells (Peterson, 2008). The abnormality of the hemoglobin is caused by a mutation in a gene of the hemoglobin protein. This abnormality hinders the proper formation globin genes of the hemoglobin molecules resulting in abnormal hemoglobin that may take the forms of “S” hemoglobin or “SC” hemoglobin or “beta-thalassemia” hemoglobin as noted by (Rees, Williams & Gladwin, 2010). Types of Sickle Cell Disease The disorders; sickle cell anemia disease (caused by “S” hemoglobin), “SC” disease (caused by “SC” hemoglobin and “S-beta thalassemia” (caused by “beta-thalassemia” hemoglobin) are collectively referred to as sickle cell disease (Rees et al, 2010). The most common form of Sickle cell disease is the Sickle cell anemia. Sickle beta-thalassemia is less common but can be either mild or severe while hemoglobin S-C disease is milder than Sickle cell anemia. Inheritance of Sickle...
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... Bonded to Hemoglobin 3. Describe the important role of the heme groups within each hemoglobin molecule. 4. Define each of the following: deoxyhemoglobin oxyhemoglobin 5. What is the oxygen association reaction that occurs in the lungs? 6. What is the oxygen dissociation reaction that occurs at the tissue cells? Factors That Affect Hemoglobin’s Saturation With Oxygen 7. Name the factors that affect hemoglobin’s saturation with oxygen. Once completely saturated, the molecule is called oxyhemoglobin. Oxygen-Hemoglobin Dissociation Curve 8. PO2 is a primary factor influencing the degree of hemoglobin saturation. Explain how PO2 in the lungs and tissue cells determines whether oxygen binding or dissociation occurs with hemoglobin. Hemoglobin’s Affinity for Oxygen 9. a. Describe the Bohr Effect. b. In contrast to the Bohr Effect, how does elevated pH affect hemoglobin’s oxygen affinity? 10. a. Actively metabolizing cells aerobically use oxygen and produce carbon dioxide. Describe how increasing levels of blood carbon dioxide affect hemoglobin’s oxygen affinity? Where (in the body) does this occur? b. Explain CO2’s affect on oxygen loading in the alveolar spaces. 11. Describe how body temperature affects O2 association with hemoglobin. 12. Explain the affect of BPG on O2 association with hemoglobin....
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...cell anemia is an inherited form of anemia — a condition in which there are not enough healthy red blood cells to carry proper amount of oxygen throughout your body. Many people may have heard about sickle cell and may be aware but many most likely do not know how it exactly works. When looking at sickle cell blood cells you can tell the differences between normal blood cells and sickle cell blood cells. Sickle cell blood cells, are crescent shaped, normal cells are more circular. Sickle cell starts off by people with sickle cell trait have red blood cells that have normal hemoglobin A, and abnormal hemoglobin. The abnormal hemoglobin is called hemoglobin S. People with sickle cell trait have more hemoglobin A than hemoglobin S. They have enough hemoglobin A to help their red blood cells carry oxygen to the body. There are three common types of sickle traits are, Sickle Cell Anemia (SS), Sickle-Hemoglobin C Disease (SC), and Sickle Beta-Plus Thalassemia and Sickle Beta Thalassemia. How exactly does someone get sickle cell? Sickle is a hereditary trait. For example, my aunt has the trait and my mom does not. My sister and I likewise do not have the trait but there is a good possibility that one of our children can. My aunt met someone else who also has the sickle cell trait and they had two children. Only one of their children has the sickle cell disease. Everyone one in four children will get the sickle disease. If one parent has sickle cell disease and the other parent doesn't...
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...Heme Groups Oxygenated Hemoglobin * Formed via transportation of O2 to cells in tissue * O2 adheres to heme protein in Hgb * T (taut state) R (relaxed state) makes binding easier or releases De-oxygenated Hemoglobin * is not bound to oxygen molecule * Higher absorption * Blue-ish in color Bohr’s Effect CO2 produced through citric acid cycle, Hg carries oxygen from lungs to body's tissues. Hg releases oxygen for CO2 and affects pH levels. Normal pH range is 7.2 - 7.4 ↓ pH causes ↑ in the amount of oxygen being released in hemoglobin. An elevated pH will cause the oxygen to bind the hemoglobin proteins in RBCs. ("Hemoglobin," n.d.) RBCs are round cells that have concaved centers. They are flexible making it easy to move through blood vessels. Sickle cell RBC's are developed from mutations in DNA - mRNA transcriptions. They are crescent shape and become fibrous. This causes them to stick to one another. Once they begin to stick, the deoxygenated cells are unable to travel to the lungs to receive oxygen. As the CO2 builds up this causes lack of oxygen to the tissues causing pain. Sickle Cell cells also cause anemia due to the fact cells die faster than normal RBCs. Sickle cell disease is an inherited autosomal recessive pattern disorder. For a child to inherit the disease both parents must have the trait and pass down a defective copy of the gene. Those who inherit one normal hemoglobin copy gene and one mutated copy...
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...return to the lungs for re-oxygenation. Oxygenated blood is bright red. Deoxygenated blood is dark red. Oxygenated blood cells have a relaxed shape whereas deoxygenated blood cells have a tense shape. 2. Carbon dioxide concentration decreases as blood nears the lungs, which in return causes and increase in pH . Increased pH causes increased affinity for oxygen which causes the hemoglobin to pick up oxygen entering your blood to be transported to the body’s tissue. Hemoglobin loses hydrogen ions from specific amino acids at key sites as pH rises causing slight changes in its structure that increase its ability to bind oxygen. As pH falls hemoglobin picks up hydrogen ions and its affinity for oxygen decreases. Increasing carbon dioxide concentration in your tissues cause a decrease in pH, which in turn forces hemoglobin to dump the oxygen it's carrying so your cells can use it for energy . a. 3. B. 1. 2. 3. Diseased cells have lower than normal ability to transport oxygen. Sickle cell hemoglobin is stiff and sticky. They stick together and do not flow through vessels easily causing blockages. The blockages caused by sickle cells affect oxygen being transported to tissues in the body. 4. a. Sickle cell disease is an inherited condition. People who receive the sickle cell gene from only parent have sickle cell trait which normally causes no health issues. People who receive...
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...the production of RBCs. This drug is made by the DNA recombinant technology with certain limitations and controlled dosage to the patients. In patients with Chronic Kidney Disease (CKD), HIV infected patients being treated by zidovudine and cancer patients being treated with chemotherapy, Epogen dosages are 50-100 units/kg thrice a week, 100 units/kg thrice a week and 600-900 units/kg thrice a week keeping an eye on hemoglobin level. Epoetin alfa (Epogen) injection is limited to use in certain conditions such as, if hemoglobin level rises to 11 g/dL ten Epogen is prohibited to administer. There are certain side effects of consuming Epogen ranging from local, gastrointestinal to dermatological. Discussion Red Blood Cells (RBCs) are the essential part of human blood which carries oxygen to the body tissues. If there is lack of sufficient healthy RBCs in the body, the condition is called Anemia, ranging from mild to severe. Anemic patient mostly feel weak and tired. Anemia is of several types among which blood loss is the most common. Deficiency of Hemoglobin...
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...solution in which red and white blood cells and platelets are floating. Plasma helps to maintain normal blood pressure and volume to supplying critical proteins for blood clotting and immunity (Blood, 2011). The function of red blood cells is to move oxygen from the lungs to body tissues. Red blood cells are formed in the red bone marrow of certain bones, and they produce a substance called hemoglobin. Hemoglobin is a protein pigment that contains iron and that gives red blood cells their color. The hemoglobin in red blood cells combines with oxygen in the lungs, transporting that oxygen to the tissues throughout the body. Red bloods cells live only about four months and new ones are continuously being produced in the bone marrow to replace the old ones (Blood, 2011). Platelets are small, disk-shaped fragments of cells that are broken off from other cells in the bone marrow. They help to control bleeding by sticking to the ruptured blood vessels and releasing substances that attract other platelets forming a temporary blood clot (Blood, 2011). Scenario One...
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...PROTEIN FUNCTION-MYOGLOBIN AND HEMOGLOBIN 208.5.3-01-05 Hemoglobin Model Comparison to Oxygenated and Deoxygenated Hemoglobin The Bohr Effect * The Bohr effect is the relationship between hemoglobin and pH’s ability to bind oxygen. I will explain this in more detail. We begin our journey in the lungs. Our lungs have the most amount of oxygen in the body. This is a good thing because our hemoglobin is strongly attracted to and has a high affinity to oxygen. The oxygen gets heavily bound to the hemoglobin and this helps to deliver the oxygen to rest of the body. The Bohr effect allows the steady release of this bound up oxygen throughout the body while the blood is delivered to the other parts of the body such as the fingers and toes. You see our pH in the lungs is around 7.4. As the blood moves through our body our pH is changed to around 7.2 because the blood picks up carbon dioxide. Carbon dioxide is produced by our cells in the citric acid cycle and each round of the citric acid cycle causes our carbon dioxide to increase. Each cell performs this citric acid cycle, which causes a lot of carbon dioxide to build up. Our blood picks the carbon dioxide up to be able to bring it back to the lungs to be blown out of the body, but as the blood is picking up carbon dioxide it is also leaving the oxygen it needs from the blood. You see the Boher effect allows this to happen. Bohr Effect Graph Hemoglobin vs. Myoglobin Sickle Cell Anemia (amino acid) Diagram Sickle Cell Anemia...
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... BIOL 1010 James Cheetham May 29 2014 Sickle Cell Anemia, Also known as Hemoglobin S Disease (HbS Disease), spreads along the lines of anemic or iron deficient blood types . Hemoglobin is the red protein that is responsible for transporting Oxygen in vertebrates. It is composed of 4 protein subunits, two called Alpha – globin and two called Beta-globin. The HBB gene, located on the 11th Chromosome (11p15.4 specifically and its locus MIM number is141900), provides “Instructions “ for making the beta globin but unfortunately nothing in life is perfect and mutations are bound to occur. Various versions of Beta Globin result from different kinds of mutations in the HBB gene. Some mutations in the HBB gene lead to abnormal versions of beta globin such as hemoglobin C (HbC) and hemoglobin E (HbE). HBB gene mutations can also result in unusually low levels of beta-globin; this abnormality is called beta thalassemia .One particular mutation produces the abnormal HbS Beta globin. People with sickle cell disease, at least one of the beta globin subunits in hemoglobin are replaced with hemoglobin S. For example, people with sickle hemoglobin C (HbSC) disease have hemoglobin molecules with hemoglobin S and hemoglobin C instead of beta globin If mutations that produce Hemoglobin S and beta thalassemia occur together, individuals have hemoglobin S-beta thalassemia (HbSBetaThal). In people with Sickle Cell Anemia, both Beta Globin subunits of Hb are replaced...
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...This paper will describe what sickle cell anemia is, how it effects the human body; as well as the oral cavity. Sickle cell anemia is a hereditary disease caused by abnormal hemoglobin, which causes the red blood cells to have low oxygen levels (National Heart, Lungs and Blood Institute, 2015). Sickle cell anemia is inherited only if both parents have the disorder because it is caused by the genetic abnormality of hemoglobin (webMD, 2015). When there is abnormal hemoglobin it can produce sickle hemoglobin (webMD, 2015). This causes the red blood cells to stick together and create long rod shaped red blood cells when oxygen leaves the cell (webMD, 2015). When this happens it causes the symptoms of sickle cell anemia (webMD, 2015). In people...
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...energy and we do not do anything to help to replace it, so our body does not produce enough red blood cells. All of these can lead to that famous, so common and dangerous disease, Anemia. According to the National Anemia Action Council, “Anemia occurs when you have a below-normal level of hemoglobin or hematocrit. Anemia can be a temporary or long-term disease, and can range from mild to severe. If you have mild anemia, there may be no symptoms or only mild symptoms, but severe anemia can result in a major impact on the quality of life”. In other words, it can also be defined as the lack of red blood cells in our body. In the following report, I am going to give a more clear explanation about what is Anemia and I am going to focus on 6 important factors about the disease which will help clarify the understanding of it. This report will be developed in the next order: Definition, Classification, Types, Causes, and Symptoms, Diagnosis, Treatment, and Cure besides other relevant information. I hope to be clear and direct with the information that I am going to provide to you. What is Anemia? In a simple way, let’s say that Anemia is an abnormally low concentration of hemoglobin in blood. Red blood cells are a very essential component in the blood. According to an article in a web page called botanical-online.com, the main function of red blood cells is the transportation of oxygen from the lungs to the cells. To...
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...differences between the oxygenated and deoxygenated states of hemoglobin. One big difference would be that the oxygenated state of hemoglobin has oxygen binding to the heme portion of the molecule. Deoxygenated hemoglobin has released the oxygen to the tissues. Hemoglobin has two states; Taut and relaxed. Deoxygenated hemoglobin is in the “T” state and Oxygenated hemoglobin is in the “R” state. Deoxygenated hemoglobin has a low affinity for oxygen in its “T” state, while Oxygenated hemoglobin binds with greater affinity. 2. Explain how pH impacts the binding and release of oxygen by hemoglobin. The way pH acts and binds and releases oxygen is called the, “Bohr effect.” The ability of hemoglobin to bind to oxygen is related to CO2 concentration. CO2 concentration is also directly related to acidity; the more CO2, the higher the acidity, which also means a lower pH level (Low pH equals high acidity). When the CO2 concentration gets higher and the pH gets lower, it causes the hemoglobin to “get rid” of the oxygen. On the flip side, when there is less CO2 and the pH increases, this causes the hemoglobin to “pick up” the oxygen. This process is also known as the, “Hemoglobin Dissociation Curve.” 3. Explain how the diseased cells differ from normal red blood cells in their capacity to transport oxygen. Normal red blood cells contain hemoglobin that assist in transporting oxygen to the whole body, referred to as Hemoglobin A. These normal cells live on average around 120 days. They...
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