when not enough hemoglobin is being made due most often to the lack of iron in the body. A way to help with this is by administering drugs, such as Epogen and Procrit, which can increase the hemoglobin level in the body. There is no one optimal hemoglobin level for everyone as it varies due to different factors, including sex, health, and lifestyle. One of the factors that cause hemoglobin levels to vary in people is the sex of an individual. There is no major difference in hemoglobin levels in prepubertal
Choice “B” is the best answer. Hemoglobin electrophoresis uses the principles of gel electrophoresis to separate out the various types of hemoglobin and is a type of native gel electrophoresis. The test can detect abnormal levels of HbS; the form associated with sickle cell disease, as well as other abnormal hemoglobinopathies such as hemoglobin C. Different hemoglobins have different charges, and according to those charges and the variable amino acid composition, hemoglobins move at different speeds in
This study was aimed to assess the hemoglobin level, and associated factors to the development of neonatal infection in Neonatal Intensive Care Unit (NICU). In our study of 256 neonates, the most prevalent diagnosis on admission was Hypoxic-Ischemic Encephalopathy (HIE) of new born (43.00%) followed by prematurity (29.70%). Birth weight (with mean=1889g,), gestational age (mean= 34.2 weeks), hospital stay (mean=12days) and hemoglobin level (mean=14±2 g/dl) had greater odds for development of neonatal
cells or hemoglobin (a polypeptide). The focus of this report will be on the lack of hemoglobin as it is the most prevalent case in most anaemic patients. The protein molecule is found in red blood cells and carries oxygen from the lungs to the body's tissues and returns carbon dioxide from the tissues back to the lungs. It is composed of four protein chains, two alpha chains and two beta chains, each with a ring-like heme group containing an iron atom. The aspects of anemia and hemoglobin that will
CHECK PLAGIARISM Hemoglobin is a protein that is found in red blood cells. It carries oxygen to different areas of the human body. Normal red blood cells are shaped like doughnuts without a hole. This shape is very flexible and allows the cells to move through large and small veins. Some people have an inherited gene that causes a slight change in the protein hemoglobin. If a person has two of these genes, then the person has a disease called sickle cell anemia. The sickle hemoglobin forms stiff rods
Introduction: On August 20, a lab was started doing different test involving blood. The objective of the experiment was to test white blood cells (WBC), red blood cells (RBC), platelet counts, differential of WBCs, a hematocrit, a hemoglobin analysis, and also various calculated indices. All the test will indicate if a person’s blood levels are normal or if the person has an abnormal blood count. To explain what blood is, blood is a red liquid that circulates throughout the body. It also transports
experiment, we are comparing the structures of fetal wild type hemoglobin (HbF) and adult wild type hemoglobin, as well as adult sickle cell hemoglobin and adult wild type hemoglobin. Fetal hemoglobin differs from adult hemoglobin because the fetal hemoglobin contains two alpha subunits and two gamma subunits, while adult hemoglobin contains two alpha subunits and two beta subunits. Sickle cell hemoglobin is different from wild type hemoglobin because there is a missense mutation that causes glutamic
Hemoglobin is present in red blood cells of the body and transport oxygen from lungs to the rest of the human body (National, 2015). Humans carry different types of hemoglobin, but there are three common types found in the gel electrophoresis. One of the test blood that help people to diagnose any disease is the hemoglobin electrophoresis. Hemoglobin electrophoresis test looks at the different types of hemoglobin in the blood, and can help diagnose the type of anemia that the person could have (National
Ana-Maria Sutac Biochemistry 370 11/13/2015 Hemoglobin and Sickle Cell Disease Introduction Sickle cell disease, also known as SCD, is a hereditary blood disorder that takes place due to mutation in the hemoglobin gene that is found in red blood cells. While it is said to have originated in Africa and is mostly predominant in African Americans, sickle cell disease is now common among different ethnic groups all over the world. Sickle cell anemia (HbSS) infects “an estimated 70,000 to 100,000
One of these is to a histidine residue which lies eight residues along helix F of hemoglobin, the proximal hitidine (His F8). The sixth bond is to one of the oxygen atoms in a molecule of oxygen. Near to where the oxygen binds to the heme group is another histidine residue, the distal histidine (His E7). This serves two very important functions. First, preventing neightboring hemoglobin molecules coming into contact with one another and oxidizing to the Fe3+ state, cause no longer bind