Albumin is the most abundant plasmatic protein as it corresponds to 50% of all the proteins found in plasma. It’s synthesised in the liver and it has a half-life of 19-21 days. Its importance lies on the multiple functions to which it has been associated to: regulates oncotic pressure, transports molecules and has a great antioxidant capacity among others. Albumin can also suffer glycation, a non-enzymatic process in/nwhich sugars are added to a molecule. This process can change albumin’s three-dimensional ...
Albumin is the most abundant plasmatic protein as it corresponds to 50% of all the proteins found in plasma. It’s synthesised in the liver and it has a half-life of 19-21 days. Its importance lies on the multiple functions to which it has been associated to: regulates oncotic pressure, transports molecules and has a great antioxidant capacity among others. Albumin can also suffer glycation, a non-enzymatic process in/nwhich sugars are added to a molecule. This process can change albumin’s three-dimensional structure affecting its antioxidant and binding capacity. In the past years, the interest in studying albumin has increased due to its possible implications in different pathologies. Healthy people have a portion of albumin which has been glycated, but this level can be overcome in diseases like diabetes. In addition, as albumin’s half-life is lower than haemoglobin’s, it allows us to determine the glycaemic fluctuations up to 3 weeks before the extraction. For this reason, it is being studied the possibility of using glycated albumin as a glycaemic marker instead of haemoglobin. In this project we will try to validate a method to determine concentrations of glycated albumin.
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