Medical/Science Study World

Abnormal Hemoglobin Hemoglobin abnormalities are the group of blood disorders that affect the normal functioning of the hemoglobin in the red blood cells. These are genetic disorders that results in the altered size and shape of the red blood cells, thereby decreasing the oxygen-carrying capacity of the blood. Hemoglobin is chains of iron-containing protein structures that comprises of alpha, beta, gamma and delta globin chains. Any change in the structure of the globin chains results in the occurrence of hemoglobin abnormalities. The common hemoglobin disorders include sickle cell anemia, thalassemia, and hemolytic anemia. Hemoglobin abnormalities is a global issue wherein 7% of the world’s population are carriers of the defective gene. Around 3- 5 lakh children are reported to be born with hemoglobin disorders each year with a large number of cases reported in low and middle-income countries. Signs and symptoms The common signs and symptoms of hemoglobin

Human hemoglobin is formed of two pairs of globin chains to each of which is attached one molecule of heme. Classification of Hemoglobin Variants    On human chromosomes, alpha type genes are located on human chromosomes No. 16 and beta type genes are clustered in human chromosome No.11. The globin chain genes have introns* between coding sequences which are removed after transcription during mRNA processing. Abnormalities in the primary sequence of globin chains would lead to hemoglobinopathies. Abnormalities in the rate of synthesis of hemoglobin would result in thalassemias.  * Introns are noncoding sections of an RNA transcript, or the DNA encoding it, that are spliced out before the RNA molecule is translated into a protein . The sections of DNA (or RNA) that code for proteins are called exons.   FUNCTION: They serve as hot spots for recombination in the formation of new combinations of exons . In other words, they are in our genes because they have been used during evolution as

Formation of Hemoglobin Synthesis of hemoglobin begins in the pro-erythroblasts and continues even into the reticulocyte stage of the red blood cells.  However, hemoglobin appears in the intermediate noroblastic stage.Therefore, when reticulocytes leave the bone marrow and pass into the blood stream, they continue to form minute quantities of hemoglobin for another day or so until they become mature erythrocytes. Heme portion of the hemoglobin is synthesized in mitochondria and the globin part is synthesized in ribosomes.  The basic chemical steps in the formation of hemoglobin.   First, succinyl-CoA, formed in the Krebs metabolic cycle, binds with glycine to form a pyrrole molecule.  In turn, four pyrroles combine to form protoporphyrin IX, which then combines with iron to form the heme molecule.  Finally, each heme molecule combines with a long polypeptide chain, a globin synthesized by ribosomes, forming a subunit of hemoglobin called a hemoglobin chain.    Each chain has a molecula

Sample Blood in   EDTA   is needed along with fresh blood smear. Definition The term leukemoid reaction describes an increased white blood cell count (< 50,000 cells/μL), which is a physiological response to stress or infection (as opposed to a primary blood malignancy, such as leukemia). It often describes the presence of immature cells such as myeloblasts or red blood cells with nuclei in the peripheral blood. It may be   lymphoid   or   myeloid . If there is a persistent increase in the neutrophils, reactive and excessive leucocytosis with a count of 30,000 to 50,000 / µL, with the presence of immature and mature white cells in the peripheral blood smear is called Leukemoid reaction. Sometimes lymphocytic reaction maybe seen. This is not primary marrow disorder, and this is due to the secondary to infections.   Significance This term is used to differentiate between the leucocytosis and leukemia. In leukocytosis or neutrophilia there is an increase in the count from 10,000 to 25,

Hemoglobin is a protein in red blood cells (RBCs).  It plays a vital role in your body. It carries oxygen from your lungs to your tissues and organs. It is a conjugated protein, & Chromoprotein. It is a chromoprotein forming 95% of dry weight of RBC and 30% to 34% of wet weight.  It is made up of Iron (haem) and Protein (globin). It also acts as a buffer and its molecular weight is 68,000. Its function is to carry the respiratory gases, oxygen and carbon dioxide. Hemoglobin is made up of four amino acid chains. Amino acids are the building blocks of proteins. Each of these chains contains heme. This is a compound that contains iron. One of the functions of heme is to transport oxygen in the bloodstream. Hemoglobin is what gives RBCs their shape. RBCs usually look like donuts, but with a thin center instead of a hole. Some conditions like sickle cell anemia can cause abnormally shaped RBCs. This can lead to serious health problems. What is the pigment in hemoglobin? Hemoglobin itsel