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Polycythemia is defined as serum hematocrit (Hct) or hemoglobin (HgB) exceeding normal ranges expected for age and sex, typically Hct >49% in healthy adult men and >48% in women, or HgB >16.5 g/dL in men or >16.0 g/dL in women. [8] The definition is different for neonates and varies by age in children. [9] [10]
A hemoglobin test measures the amount of hemoglobin in your blood. If a hemoglobin tests shows that a person's levels are below normal, it means they have a low red blood cell count, which is known as anemia. If the test shows higher levels than normal, it means they have hemoglobinemia. [citation needed] The normal range for hemoglobin is:
high-altitude pulmonary edema: HAV: hepatitis A virus Hb: hemoglobin: HB: heart block: Hb% hemoglobin concentration in gram per deciliter HbA: hemoglobin A (commonest type of hemoglobin) HbA1c: glycated hemoglobin (used as a measure of diabetes control) HBD: has been drinking HbF: fetal hemoglobin: HBO: hyperbaric oxygen: HBP: high blood ...
Hematocrit levels that are too high or too low can indicate a blood disorder, dehydration, or other medical conditions. [4] An abnormally low hematocrit may suggest anemia, a decrease in the total amount of red blood cells, while an abnormally high hematocrit is called polycythemia. [5] Both are potentially life-threatening disorders.
Hemoglobinuria is a condition in which the oxygen transport protein hemoglobin is found in abnormally high concentrations in the urine. [1] The condition is caused by excessive intravascular hemolysis, in which large numbers of red blood cells (RBCs) are destroyed, thereby releasing free hemoglobin into the plasma. [2]
The levels of glycated hemoglobin are therefore measured in order to monitor the long-term control of the chronic disease of type 2 diabetes mellitus (T2DM). Poor control of T2DM results in high levels of glycated hemoglobin in the red blood cells. The normal reference range is approximately 4.0–5.9%.
Elevated levels of methemoglobin in the blood are caused when the mechanisms that defend against oxidative stress within the red blood cell are overwhelmed and the oxygen carrying ferrous ion (Fe 2+) of the heme group of the hemoglobin molecule is oxidized to the ferric state (Fe 3+). This converts hemoglobin to methemoglobin, resulting in a ...
The hemoglobin was named hemoglobin III, [24] but hemoglobin C was eventually used. [ 25 ] [ 26 ] By 1954, it was found that the mutant hemoglobin was highly prevalent in West Africa. [ 27 ] [ 28 ] In 1960, Vernon Ingram and J. A. Hunt at the University of Cambridge discovered that the mutation was a single amino acid replacement of glutamic ...