Purpose

A low hemoglobin measurement usually means the person has anemia. Anemia results from a decrease in the number, size, or function of RBCs. Common causes include excessive bleeding, a deficiency of iron, vitamin B 12 , or folic acid, destruction of red cells by antibodies or mechanical trauma, and structurally abnormal hemoglobin. Hemoglobin levels are also decreased due to cancer, kidney diseases, other chronic diseases, and excessive IV fluids. Hemoglobin levels are also used to determine if a person needs a blood transfusion . Usually a person's hemoglobin must be below 78 g/dL before a transfusion is considered, or higher if the person has heart or lung disease. The hemoglobin concentration is also used to determine how many units of packed red blood cells should be transfused. A common rule of thumb is that each unit of red cells should increase the hemoglobin by approximately 1.01.5 g/dL. Certain drugs such as antibiotics , aspirin , antineo-plastic drugs, doxapram, indomethacin, sulfonamides , primaquine, rifampin, and trimethadione, may also decrease the hemoglobin level.

Description
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 (Fe 2+ ) 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. Hemoglobin is most commonly measured in whole blood. Hemoglobin measurement is most often performed as part of a complete blood count (CBC), a test that includes counts of the red blood cells, white blood cells, and platelets (thrombocytes).

Some people inherit hemoglobin with an abnormal structure. The abnormal hemoglobin results from a point mutation in one or both genes that code for the alpha or beta polypeptide chains. Examples of hemoglobin abnormalities resulting from a single amino acid substitution in the beta chain are sickle cell and hemoglobin C disease. Most abnormal hemoglobin molecules can be detected by hemoglobin electrophoresis, which separates hemoglobin molecules that have different electrical charges.