Professional Documents
Culture Documents
Definition
Hemoglobinopathy: A genetic defect that results in
abnormal structure of one of the globin chains of the hemoglobin molecule.
Hemoglobin (Hb or Hgb) is found in all red blood cells. A hemoglobin they contain molecule is made up of heme, an iron-containing complex, and globin, protein chains that surround the heme complex. The types of protein chains found in the hemoglobin molecule affect its structure and function. Different types of hemoglobin are classified according to the type of protein chains.
Hgb A2 (alpha2-delta2) Hgb F (alpha2-gamma2) Hgb M Hgb S Hgb C Hgb E Hgb D-Punjab Hgb O-Arab Hgb G-Philadelphia Hgb Hasharon Hgb Korle-Bu Hgb Lepore
Thalassemia
The defect may affect the , , , , or epsilon chain, or may affect some combination of the chain in the same patient (but never the and chain together). The result is an imbalance in production of globin chains and the production of an inadequate number of red cells. The cells which are produced are hypochromic/microcytic and contain a surfeit of the unaffected chains which cannot stoichiometrically "mate" with the inadequate supply of thalassemic chains. These "bachelor" chains can produce adverse effects on the red cell and lead to destruction of the red cell in the marrow (ineffective erythropoiesis) and in the circulation (hemolysis). Some hemoglobinopathies may also be thalassemias, in that a structurally abnormal hemoglobin (hemoglobinopathy) may also be underproduced (thalassemia). Some, but not all, hemoglobinopathies and thalassemias are hemolytic anemias.
Hemoglobin Structure
Decreased O2 affinity These hemoglobins are reluctant to pick up O2 from the lung.
Hb Seattle, Hb Vancouver, and Hb Mobile.
Methemoglobinemia special class of low O2 affinity hemoglobin variants affected patients have cyanosis, since the methemoglobin is useless in O2 binding
Hb MSaskatoon and Hb MKankakee
Hemoglobin E
Rbc Morphology
Hb AC
Rbc Morphology
Hemoglobin H
Hb Electrophoresis
RBC Indices