LYCOS RETRIEVER 
Hemoglobin
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Hemoglobin A1c (A1c), a test which measures a person's average blood glucose level over the past 2 to 3 months, is the current "gold standard" indicator of diabetes management. Bush emphasized, "landmark studies have found that every percentage drop in A1c cuts an individual's risk for debilitating and costly diabetic complications such as retinopathy, nephropathy, and neuropathy by about one-third."
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Hemoglobin is a complex protein composed of four subunits. Each subunit consists of a protein, or polypeptide chain, that enfolds a heme group. Each heme contains iron (Fe2+) that can bind a molecule of oxygen. The iron gives blood its red color. After the first year of life, 95-97% of the hemoglobin molecules contain two pairs of polypeptide chains designated alpha and beta. This form of hemoglobin is called hemoglobin A.
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Hemoglobin has a normal concentration of 150g/liter of blood permits whole blood to carry 65 times more oxygen than does plasma at a PO2 of 100 mmHG. Hematocrit determines the fraction of the blood that is red blood cells. The red blood cells are primarily composed of hemoglobin (95% of the dry mass).
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Hemoglobin is a [H]eme containing protein responsible for transporting oxygen in the bloodstream. The heme in hemoglobin is in the form of an iron complexed with protoporphyrin IX. The protection of an oxygen-binding metal from irreversible oxidation is the functional reason for the existence of myoglobin and hemoglobin. These two molecules provide environments in which the first step of an oxidation reaction (the binding of oxygen) is permitted, but the final step (oxidation) is blocked.
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Hemoglobin (or haemoglobin, frequently abbreviated as Hb), which is contained in red blood cells, serves as the oxygen carrier in blood. The name hemoglobin comes from heme and globin, since each subunit of hemoglobin is a globular protein with an embedded heme (or haem) group. Each heme group contains an iron atom, and this is responsible for the binding of oxygen. The presence of hemoglobin in blood increases the oxygen carrying ability of a litre of blood from 5 to 250 ml. Hemoglobin ... plays a major role in the transport of carbon dioxide from the tissues back to the lungs. Myoglobin, on the other hand, is located in muscle, and serves as a reserve supply of oxygen and also facilitates the movement of O2 within muscle.
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Hemoglobin is found in the red blood cells of the body. Each red blood cell (RBC) contains approximately 280 million hemoglobin molecules (Sears, 1999). The main function of hemoglobin is to transport oxygen from the lungs to the tissues and then transport CO2 back from the tissues to the lungs. One hemoglobin molecule has the ability to transport up to 4 oxygen molecules. There are two forms of hemoglobin: oxyhemoglobin, which is saturated with oxygen molecules and deoxyhemoglobin, which is desaturated with oxygen molecules (Sears, 1999). Oxyhemoglobin has a higher affinity for oxygen than deoxyhemoglobin, and deoxyhemoglobin has a higher affinity for CO2 than oxyhemoglobin.
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Hemoglobin