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Once a hemoglobin molecule is glycated, it remains that way. A buildup of glycated hemoglobin within the red cell, therefore, reflects the average level of glucose to which the cell has been exposed during its life-cycle. Measuring glycated hemoglobin assesses the effectiveness of therapy by monitoring long-term serum glucose regulation.
The term DNA glycation applies to DNA damage induced by reactive carbonyls (principally methylglyoxal and glyoxal) that are present in cells as by-products of sugar metabolism. [13] Glycation of DNA can cause mutation, breaks in DNA and cytotoxicity. [13] Guanine in DNA is the base most susceptible to glycation. Glycated DNA, as a form of ...
Hemoglobin Barts (γ 4) – A variant form of hemoglobin, formed by a tetramer of γ chains, which may be present in variants of α thalassemia. Hemoglobin S (α 2 β S 2) – A variant form of hemoglobin found in people with sickle cell disease. There is a variation in the β-chain gene, causing a change in the properties of hemoglobin, which ...
Each hemoglobin molecule carries four heme groups; hemoglobin constitutes about a third of the total cell volume. Hemoglobin is responsible for the transport of more than 98% of the oxygen in the body (the remaining oxygen is carried dissolved in the blood plasma). The red blood cells of an average adult human male store collectively about 2.5 ...
Hemoglobin is an iron-containing protein that gives red blood cells their color and facilitates transportation of oxygen from the lungs to tissues and carbon dioxide from tissues to the lungs to be exhaled. [3] Red blood cells are the most abundant cell in the blood, accounting for about 40–45% of its volume.
The Amadori rearrangement is an organic reaction describing the acid or base catalyzed isomerization or rearrangement reaction of the N-glycoside of an aldose or the glycosylamine to the corresponding 1-amino-1-deoxy-ketose. [1]
Glycosylation also plays a role in cell-to-cell adhesion (a mechanism employed by cells of the immune system) via sugar-binding proteins called lectins, which recognize specific carbohydrate moieties. [2] Glycosylation is an important parameter in the optimization of many glycoprotein-based drugs such as monoclonal antibodies. [6]
The most famous mutation in the globin fold is a change from glutamate to valine in one chain of the hemoglobin molecule. This mutation creates a "hydrophobic patch" on the protein surface that promotes intermolecular aggregation, the molecular event that gives rise to sickle-cell disease. [citation needed]