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Glycated hemoglobin (also called glycohemoglobin) is a form of hemoglobin (Hb) that is chemically linked to a sugar. ("Glycosylated haemoglobin" is a misnomer because glycation and glycosylation are different processes, of which only the former is relevant in this case; glycation is non-enzymatic, while glycosylation is enzymatic.)
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 ...
The reaction is associated with the amino-carbonyl reactions (also called glycation reaction, or Maillard reaction) [3] in which the reagents are naturally occurring sugars and amino acids. One study demonstrated the possibility of Amadori rearrangement during interaction between oxidized dextran and gelatine.
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]
Image source: Getty Images. 1. Lockheed Martin. After its stock price reached an all-time high earlier this year, Lockheed Martin and its defense contractor peers have sold off considerably over ...
The blaze started around 2 p.m. at Little Mountain Drive near Edgehill Drive as a series of destructive and deadly infernos have engulfed parts of Los Angeles and the surrounding area.
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]