SHEEP ANTI HUMAN HEMOGLOBIN

HEMOGLOBIN

Phosphate buffered saline pH7. 4

Native from erythrocytes

Involved in oxygen transport from the lung to the various peripheral tissues. Ref. 35LVV-hemorphin-7 potentiates the activity of bradykinin causing a decrease in blood pressure. Ref. 35Subunit structureHeterotetramer of two alpha chains and two beta chains in adult hemoglobin A (HbA). Tissue specificityRed blood cells. Post-translational modificationGlucose reacts non-enzymatically with the N-terminus of the beta chain to form a stable ketoamine linkage. This takes place slowly and continuously throughout the 120-day life span of the red blood cell. The rate of glycation is increased in patients with diabetes mellitus. S-nitrosylated; a nitric oxide group is first bound to Fe2+ and then transferred to Cys-94 to allow capture of O2. Acetylated on Lys-60 Lys-83 and Lys-145 upon aspirin exposure. Ref. 34 reports the identification of HBB acetylated on Lys-145 in the cytosolic fraction of HeLa cells. This may results from a contamination of the sample. Involvement in diseaseDefects in HBB may be a cause of Heinz body anemias [MIM:140700]. This is a form of non-spherocytic hemolytic anemia of Dacie type 1. After splenectomy which has little benefit basophilic inclusions called Heinz bodies are demonstrable in the erythrocytes. Before splenectomy diffuse or punctate basophilia may be evident. Most of these cases are probably instances of hemoglobinopathy. The hemoglobin demonstrates heat lability. Heinz bodies are observed also with the Ivemark syndrome (asplenia with cardiovascular anomalies) and with glutathione peroxidase deficiency. Defects in HBB are the cause of beta-thalassemia (B-THAL) [MIM:604131]. A form of thalassemia. Thalassemias are common monogenic diseases occurring mostly in Mediterranean and Southeast Asian populations. The hallmark of beta-thalassemia is an imbalance in globin-chain production in the adult HbA molecule. Absence of beta chain causes beta(0)-thalassemia while reduced amounts of detectable beta globin causes beta+-thalassemia. In the severe forms of beta-thalassemia the excess alpha globin chains accumulate in the developing erythroid precursors in the marrow. Their deposition leads to a vast increase in erythroid apoptosis that in turn causes ineffective erythropoiesis and severe microcytic hypochromic anemia. Clinically beta-thalassemia is divided into thalassemia major which is transfusion dependent thalassemia intermedia (of intermediate severity) and thalassemia minor that is asymptomatic. Ref. 52Defects in HBB are the cause of sickle cell anemia [MIM:603903]; also known as sickle cell disease. Sickle cell anemia is characterized by abnormally shaped red cells resulting in chronic anemia and periodic episodes of pain serious infections and damage to vital organs. Normal red blood cells are round and flexible and flow easily through blood vessels but in sickle cell anemia the abnormal hemoglobin (called Hb S) causes red blood cells to become stiff. They are C-shaped and resembles a sickle. These stiffer red blood cells can led to microvascular occlusion thus cutting off the blood supply to nearby tissues. Defects in HBB are the cause of beta-thalassemia dominant inclusion body type (B-THALIB) [MIM:603902]. An autosomal dominant form of beta thalassemia characterized by moderate anemia lifelong jaundice cholelithiasis and splenomegaly marked morphologic changes in the red cells erythroid hyperplasia of the bone marrow with increased numbers of multinucleate red cell precursors and the presence of large inclusion bodies in the normoblasts both in the marrow and in the peripheral blood after splenectomy. Ref. 52Miscellaneous: One molecule of 2 3-bisphosphoglycerate can bind to two beta chains per hemoglobin tetramer. Sequence similaritiesBelongs to the globin family. Mass spectrometryMolecular mass is 1310 Da from positions 33 - 42. Determined by FAB. Ref. 21 1. Wang C. et al. (1996) Immunohistochemical study of amoeboid microglial cells in fetal rat brain. J. Anat. 189: 567 - 574. 2. Jefferies W. A. et al. (1985) Authentic T helper CD4 (W3/25) antigen on rat peritoneal macrophages. J. Exp. Med. 162:117-127. [1] \" Peptide and nucleotide sequences of rat CD4 (W3/25)