| Papers [1-8] of 8 | Search results on "HEMOGLOBIN": |
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Hemoglobin, Oxygen Transport and Nitric Oxide, 2001.
This paper presents electron paramagnetic resonance and oxygen binding studies of -nitrosyl hemoglobin - a novel oxygen carrier having NO (Nitric Oxide) assisted allosteric functions.
1,345 words (approx. 5.4 pages), 3 sources, APA, AU$ 66.95
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Abstract
This paper shows that Nitric Oxide (NO) is a very popular compound to investigate in the scientific community today. It is physiologically ubiquitous as a potent vasodilator, neurotransmitter, and immuno-active agent at low concentrations and it is produced and recycled in the respiratory tract to regulate the airway. This paper discusses in detail the mechanism behind oxygen binding and release by hemoglobin as it relates NO bound to the Hemoglobin. The oxygen affinity dynamics of native Hemoglobin and nitrosylated Hb are compared. The research also reveals that although NO has a much higher affinity than oxygen or carbon monoxide for Hemoglobin, NO behaves differently than these other ligands and is not as toxic to normal Hb oxygen binding as previously assumed.
From the Paper
"Small, unicellular aerobic organisms can obtain oxygen required for metabolism by simple diffusion from the environment. Most multicellular organisms have too great a surface area and many cells not in contact with the environment. They require circulatory systems that transport oxygen from gas-exchange organs to other tissues. In vertebrates, oxygen is bound to molecules of Hemoglobin (Hb) or transport in Red Blood Cells. Mammalian Hemoglobin is a tetramer, consisting of four polypeptide chains; two a and two b. Six ligands are coordinated to the ferrous iron, with the ligands in octahedral geometry around the metal cation (figure 1). In aqueous solution, free heme does not does not reversibly bind oxygen. Instead the Fe(II) is rapidly oxidized to Fe(III) when it gives up an electron to oxygen. The quaternary structure of hemoglobin prevents formal transfer of an electron and allows it to reversibly bind O2. Positively charged amino acid residues stabilize to negatively charged diatomic oxygen without an ionic bond. Hemoglobin unbound to oxygen is called deoxyhemoglobin and has a low affinity for oxygen. Once one oxygen molecule binds to the Fe, the proximal Histadine (figure 1) moves closer to the porphyrin ring because the Fe is now bound to six ligands instead of five. This disrupts the stabilizing ions that interact with Hb. The remaining Heme groups have an increased affinity for Oxygen. In addition to this positive cooperatively of binding, allosteric interactions regulate the binding and release of oxygen by Hb (Horton, 1996)."
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Hemoglobin, 2003.
This paper discusses the chemical structure and function of hemoglobin.
1,150 words (approx. 4.6 pages), 5 sources, MLA, AU$ 57.95
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Abstract
This paper explains how hemoglobin works. The author describes the oxygen-carrying capacity of different hemoglobins and what affects it. The paper relates the way hemoglobin acts in different under different physiologic conditions.
From the Paper
"Hemoglobin is an oxygen-carrying protein and acts as such in most mammals. Typically hemoglobins have a tetrameric structure consisting of two polypeptide chains of amino acids each and two polypeptide chains of amino acids each with each subunit ..."
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Variants of Hemoglobin, 2002.
This paper discusses the main hemoglobin variants, their properties and the effects of said variants.
2,162 words (approx. 8.6 pages), 6 sources, MLA, AU$ 98.95
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Abstract
A thorough discussion of the main variants of hemoglobin, their structures, effects and biochemical signifigance. The discussion of the hemoglobin mutants also involves the diseases associated with them, as well as the symptoms and treatments of these disease.
From the Paper
"Hemoglobin is an extremely important molecule to the life processes of animals. Hemoglobin functions to transfer oxygen from the lunge to the individual cells of the body, allowing respiration to occur, and providing the oxygen necessary for life functions. Hemoglobin comes in many different forms and each change in structure effects the overall function of hemoglobin. How each type of change specifically changes the function of hemoglobin is important to understand how hemoglobin works as well as for treatment in diseases caused by hemoglobin mutants."
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Sickle Cell Anemia, 2004.
An analysis of sickle cell anemia, an inherited blood disorder of defective hemoglobin.
1,065 words (approx. 4.3 pages), 8 sources, MLA, AU$ 54.95
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Abstract
This paper discusses the inherited blood disorder of sickle cell anemia. The paper presents the statistics of the prevalence of this disorder in the United States and outlines the populations that are most affected by the disease. The paper examines the genotypic and phenotypic expressions of the sickle cell trait. The paper explores the belief that sickle hemoglobin evolved as a protection against malaria.
From the Paper
"Sickle cell anemia is an inherited blood disorder in which hemoglobin is defective (Genetic disease profile: Sickle cell anemia). After hemoglobin molecules give up their oxygen, some cluster together and form long, rod-like structures. These structures cause red blood cells to become stiff and assume a sickle shape that makes it difficult for them to squeeze through small blood vessels. As a result, they stack up and cause blockages that deprive organs and tissues of oxygen-carrying blood. Sickle cell anemia affects millions world wide (Genetic disease profile: Sickle cell anemia). It is the most common among people whose ancestors come from sub-Saharan Africa; Spanish-speaking regions (South America, Cuba, Central America); Saudi Arabia; India; and Mediterranean countries such as Turkey, Greece, and Italy."
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Immune Thrombocytopenic Purpura, 2001.
An overview of the hemoglobin disorder, Immune Thrombocytopenic Purpura (ITP).
1,235 words (approx. 4.9 pages), 5 sources, APA, AU$ 62.95
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Abstract
This paper explains the causes, symptoms, and treatments of Immune Thrombocytopenic Purpura (ITP) from both a biological and a patient?s perspective. It also touches upon the differences between the ways ITP occurs in children and adults and the complications the ailment can cause during pregnancy.
From the Paper
"Pregnancy is also a common cause of ITP. Abdul Rahim Gari-Bai, Fachartz, a noted hematologist, writes in a recent review article, that as platelets play a particularly important role in primary and secondary hemostasis during pregnancy, any decrease in their count in peripheral blood is a cause for considerable concern. Bleeding problems are especially common during the first and third trimester, as well as during and after delivery. Furthermore, the child the woman is carrying may be affected by maternal Thrombocytopenia. This is especially dangerous because babies are subject to great stress during the passage through the birth canal."
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Blood Substitutes in Development, 2004.
An overview of the blood shortage and potential life-supporting alternatives.
1,253 words (approx. 5.0 pages), 1 source, MLA, AU$ 62.95
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Abstract
This paper discusses how there is a fear, which continues today, regarding safe blood and HIV and how beyond contamination, there is another serious blood issue and that involves blood shortages. It describes the actual function of the blood to the body, how blood cells regenerate, and the principles of blood transfusions. It shows that duplicating all the functions that blood performs in the human body would seem to be an impossible challenge and how any artificial blood product must pass several tests. It also looks at current research into synthetic blood production from two distinct directions, one based on chemicals and the other based on hemoglobin.
From the Paper
"What function does blood actually provide within ? and for ? the body? According to the assigned article in Scientific American, blood ?transports nutrients, hormones and waste products?; blood also fights infections and has the ability to ?clot? ? preventing or at least slowing down serious hemorrhaging. The part of human blood which helps fight disease is the white blood cells. But the most ?familiar? function of blood in the body of mammals is the ?capture and release of oxygen and carbon dioxide.? The protein most commonly found in blood, hemoglobin, is also a critically important protein. Hemoglobin picks up oxygen in the lungs, and distributes it throughout the body. The red blood cells pick up carbon dioxide, which is a waste product given off through the respiration of cells, and humans exhale the carbon dioxide out through the lungs."
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The Biochemistry of Lead Poisoning, 2003.
A look at the chemical mechanisms and biological effects of lead poisoning.
1,395 words (approx. 5.6 pages), 9 sources, MLA, AU$ 68.95
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Abstract
This paper describes lead poisoning, focusing on the chemical processes that take place as lead (II) displaces zinc (II) from ALAD and inhibits hemoglobin synthesis. The technical details of the inorganic and biochemical processes at play are explored and discussed, as well as the mechanisms of various lead poisoning therapeutic strategies. This paper also contains several referenced illustrations and figures.
From the Paper
"The protein ALAD, also know as porphobilinogen, is crucial in heme biosynthesis (2). ALAD, a ZnII metalloenzyme, consists of A and B subunits each of which contain a zinc atom when functional. The functionality of the A and B sites has been determined experimentally by displacement of zinc. When magnesium displaces zinc at the A site ALAD is marginally active. Furthermore, when magnesium replaces the zinc in the B site no change in the activity of the enzyme is observed (3). Thus the A site is key to the activity of the enzyme. However, when PbII displaces the active ZnII ion present in the A- site, the enzyme is rendered useless."
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