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Electroforese en xel bidimensional: Diferenzas entre revisións

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Liña 5:
 
== Base para a separción ==
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2-D [[electrophoresis]] begins with electrophoresis in the first dimension and then separates the molecules perpendicularly from the first to create an electropherogram in the second dimension. In electrophoresis in the first dimension, molecules are separated linearly according to their isoelectric point. In the second dimension, the molecules are then separated at 90 degrees from the first electropherogram according to molecular mass. Since it is unlikely that two molecules will be similar in two distinct properties, molecules are more effectively separated in 2-D electrophoresis than in 1-D electrophoresis.
 
A [[electroforese]] 2-D empea cunha electroforese na primeira dimensión e despois separa as moléculas perpendicularmente desde a primeira para crear un electroferograma na segunda dimensión. Na electroforese na primeira dimensión as moléculas sepáranse linearmente segundo o seu [[punto isoeléctrico]]. Na segunda dimensión as moléculas son separadas a 90 graos desde o primeiro electroferograma segundo a súa masa molecular. Como é improbable que dúas moléculas sexan similares en dúas propiedades distintas, as moléculas son separadas con maior efectividade na electroforese 2-D que na 1-D.
The two dimensions that proteins are separated into using this technique can be [[isoelectric point]], protein complex mass in the [[native PAGE|native]] state, or protein [[mass]].
 
As dúas dimensións nas que se separan as proteínas usando esta técnica poden ser o seu punto isoeléctrico, masa do complexo proteico en estado [[PAGE nativa|nativo]], ou a masa da proteína.
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Separation of the proteins by isoelectric point is called [[isoelectric focusing]] (IEF). Thereby, a gradient of pH is applied to a gel and an electric potential is applied across the gel, making one end more positive than the other. At all pH values other than their isoelectric point, proteins will be charged. If they are positively charged, they will be pulled towards the more negative end of the gel and if they are negatively charged they will be pulled to the more positive end of the gel. The proteins applied in the first dimension will move along the gel and will accumulate at their isoelectric point; that is, the point at which the overall charge on the protein is 0 (a neutral charge).
 
Liña 44:
For an overview of the current approach for software analysis of 2DE gel images see<ref>{{cite journal |vauthors=Berth M, Moser FM, Kolbe M, Bernhardt J |title=The state of the art in the analysis of two-dimensional gel electrophoresis images |journal=Appl. Microbiol. Biotechnol. |volume=76 |issue=6 |pages=1223–43 |date=October 2007 |pmid=17713763 |pmc=2279157 |doi=10.1007/s00253-007-1128-0 }}</ref> or.<ref>{{cite journal |vauthors=Bandow JE, Baker JD, Berth M, etal |title=Improved image analysis workflow for 2-D gels enables large-scale 2-D gel-based proteomics studies--COPD biomarker discovery study |journal=Proteomics |volume=8 |issue=15 |pages=3030–41 |date=August 2008 |pmid=18618493 |doi=10.1002/pmic.200701184 |url=http://www3.interscience.wiley.com/journal/120749796}}</ref>
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== Notas ==
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Traído desde «https://gl.wikipedia.org/wiki/Electroforese_en_xel_bidimensional»