Clinical significance of hemoglobin in hematology analyzer

　　 Hemoglobin, also known as hemoglobin, is the main component of red blood cells and can combine with oxygen to transport oxygen and carbon dioxide. The hemoglobin content can well reflect the normal range of anemia for male and female newborns 170~200g/L (17.0-20.0g/dl).

　　Introduction of inspection Hemoglobin, also known as hemoglobin, is the main component of red blood cells and can combine with oxygen to transport oxygen and carbon dioxide.

　　Clinical significance of the clinical significance of hemoglobin increased and decreased by hematology analyzer is basically similar to the clinical significance of red blood cell count, but hemoglobin can better reflect the degree of anemia.

Increased hemoglobin has the following conditions: physiological increase: seen in plateau residents, fetuses and newborns, vigorous activity, fear, cold water bath, etc.; pathological increase: seen in severe congenital and acquired cardiopulmonary diseases and vascular malformations, such as French fourth Comorbidities, cyanotic congenital heart disease, obstructive emphysema, pulmonary heart disease, pulmonary artery fistula or pulmonary vein fistula, and abnormal hemoglobin disease with low oxygen carrying capacity; also seen in certain tumors or kidney diseases, such as kidney cancer , Hepatocellular carcinoma, renal embryomas, hydronephrosis, polycystic kidney, etc.

　　Hemoglobin reduction can be seen in the following situations: Physiological reduction: 3 months of infants to children before the age of 15, mainly due to the relatively insufficient hematopoietic hematopoietic system due to rapid growth and development, generally 10%-20% lower than normal people. During the second and third trimesters of pregnancy, the blood volume is diluted due to the increase in blood volume during pregnancy. In the elderly, the hematopoietic function of the bone marrow gradually decreases, which can lead to a decrease in the content of red blood cells and hemoglobin.

Pathological reduction: bone marrow hematopoietic failure, such as anemia associated with aplastic anemia and bone marrow fibrosis; anemia due to lack of hematopoietic substances or utilization disorders, such as iron deficiency anemia, folic acid and vitamin B12 deficiency Megaloblastic anemia; anemia caused by excessive destruction of red blood cells caused by defects in red blood cell membranes, enzymes or external factors, such as hereditary spherical polycythemia, marine anemia, paroxysmal nocturnal hemoglobinuria, abnormality Hemolytic disease, immune hemolytic anemia, major surgery for cardiopulmonary bypass or certain biological and chemical factors, and hemolytic anemia caused by certain factors such as acute or chronic blood loss.

　　 Introduction of Hb molecular structure of blood cell analyzer Each 1Hb molecule is composed of 1 globin and 4 heme (also known as ferrous protoporphyrin). Each heme is composed of 4 pyrrolyl groups, and the center is an iron atom. Each globin has 4 polypeptide chains, and each polypeptide chain is connected with at least one hemoglobin to form the monomer or subunit of Hb. Hb is a tetramer composed of 4 monomers. The composition of the globin polypeptide chains of different Hb molecules is different. The polypeptide chain of adult Hb (HbA) is 2 α chains and 2 β chains, which is α2β2 structure. Fetal Hb (HbF) is composed of 2 α chains and 2 γ chains, and has an α2γ2 structure. Shortly after birth, HbF was replaced by HbFA. The sequence of amino acids in the polypeptide chain is already clear. Each alpha chain contains 141 amino acid residues, and each beta chain contains 146 amino acid residues. The Fe2+ of heme is connected to the amino acid residues of the polypeptide chain. If this histidine residue is replaced by other amino acids or the adjacent amino acids are changed, it will affect the function of Hb. EEG machines show that protein structure and function are closely related.