A Change in Hemoglobin's Structure Can Disturb Hemoglobin Function

Changes in the structure of hemoglobin may disrupt the summary of hemoglobin function: the fact that molecular structure determines its function can be seen by oxygen transporter hemoglobin. Hemoglobin can take two forms, an oxygen state and a deoxygenated state, and each form has a different function for hemoglobin. In normal hemoglobin, oxygen binds to the heme group during the oxygen state and releases oxygen during the deoxygenation state. However, when hemoglobin is mutated like sickle cell anemia, the amino acid glutamic acid is substituted by valine at the 6th position of the β subunit; hemoglobin does not normally function in the deoxygenated state.

Hemoglobin C (Hb C) is one of the most common structural hemoglobin variants in the human population. People with the hemoglobin C trait (Hb AC) have a normal phenotype without clinically significant limitations or symptoms, while those with hemoglobin C disease (Hb CC) develop mild hemolytic anemia, splenomegaly and margin . Although the clinical complications of anemia hemoglobin C disease are not serious, the heredity of other hemoglobin diseases such as hemoglobin S may have serious consequences, and genetic counseling and predictive guidance are important in providing care to these people It plays an important role.

People with the characteristics of hemoglobin C have red blood cells, normal hemoglobin A, and abnormal hemoglobin. Hemoglobin C Hemoglobin C trait, called human hemoglobin A, is slightly higher than hemoglobin C. People with traits of hemoglobin C have no health problems associated with traits. Characteristics of hemoglobin C are handed down from parents' parents such as hair color and eye color. If one parent has hemoglobin C profile and the other parent has normal hemoglobin, the probability of having a child unique to hemoglobin C for every pregnancy is 50% (1/2). These are possible results for each pregnancy

Hemoglobin is composed of subunits, and the protein structure is called a quaternary structure. Each of the four subunits constituting hemoglobin is arranged in a ring in which iron atoms are covalently bonded to heme at the center of each subunit. Binding of the first oxygen molecule results in a conformational change in hemoglobin that allows the second oxygen molecule to bind more readily. As each oxygen molecule binds, it further promotes the binding of the next molecule until all four heme sites are occupied by oxygen. You can say the opposite. When the first oxygen molecule dissociates and "falls" out of the tissue, the next oxygen molecule becomes easy to dissociate. Hemoglobin is considered to be saturated when all four heme sites are occupied. When occupying 1 to 3 heme sites, hemoglobin is said to be partially saturated.