dc.contributor.author |
Grifols i Vilella, Carlota |
dc.date |
2015-07-27 |
dc.identifier.uri |
http://hdl.handle.net/10230/24656 |
dc.format |
application/pdf |
dc.language.iso |
eng |
dc.rights |
Attribution-NonCommercial 3.0 Spain |
dc.rights |
info:eu-repo/semantics/openAccess |
dc.rights |
http://creativecommons.org/licenses/by-nc/3.0/es/ |
dc.subject |
Albúmina |
dc.subject |
Glicosilació |
dc.title |
Development of a method to assess glycated albumin |
dc.type |
info:eu-repo/semantics/bachelorThesis |
dc.description.abstract |
Treball de fi de grau en Biologia Humana |
dc.description.abstract |
Directora/supervisora del treball: Montse Costa |
dc.description.abstract |
Tutor UPF: Fèlix Bosch |
dc.description.abstract |
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. |