<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-06-26T20:12:27Z</responseDate><request verb="GetRecord" identifier="oai:docta.ucm.es:20.500.14352/93429.2" metadataPrefix="mods">https://docta.ucm.es/rest/oai/request</request><GetRecord><record><header><identifier>oai:docta.ucm.es:20.500.14352/93429.2</identifier><datestamp>2025-03-18T15:37:46Z</datestamp><setSpec>com_20.500.14352_14</setSpec><setSpec>col_20.500.14352_15</setSpec></header><metadata><mods:mods xmlns:mods="http://www.loc.gov/mods/v3" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-1.xsd">
   <mods:name>
      <mods:namePart>Maestro García-Donas, María Beatriz</mods:namePart>
   </mods:name>
   <mods:name>
      <mods:namePart>Velasco, Isabel</mods:namePart>
   </mods:name>
   <mods:name>
      <mods:namePart>Castillejo, Isabel</mods:namePart>
   </mods:name>
   <mods:name>
      <mods:namePart>Arevalo-Rodriguez, Miguel</mods:namePart>
   </mods:name>
   <mods:name>
      <mods:namePart>Cebolla, Ángel </mods:namePart>
   </mods:name>
   <mods:name>
      <mods:namePart>Sanz, Jesús</mods:namePart>
   </mods:name>
   <mods:extension>
      <mods:dateAvailable encoding="iso8601">2024-01-23T15:29:13Z</mods:dateAvailable>
   </mods:extension>
   <mods:extension>
      <mods:dateAccessioned encoding="iso8601">2024-01-16T15:58:30Z</mods:dateAccessioned>
   </mods:extension>
   <mods:originInfo>
      <mods:dateIssued encoding="iso8601">2008</mods:dateIssued>
   </mods:originInfo>
   <mods:identifier type="citation">Maestro, Beatriz, et al. «Affinity Partitioning of Proteins Tagged with Choline-Binding Modules in Aqueous Two-Phase Systems». Journal of Chromatography A, vol. 1208, n.o 1-2, octubre de 2008, pp. 189-96. https://doi.org/10.1016/j.chroma.2008.08.106.</mods:identifier>
   <mods:identifier type="issn">0021-9673</mods:identifier>
   <mods:identifier type="doi">10.1016/j.chroma.2008.08.106</mods:identifier>
   <mods:identifier type="uri">https://hdl.handle.net/20.500.14352/93429.2</mods:identifier>
   <mods:identifier type="essn">1873-3778</mods:identifier>
   <mods:identifier type="officialurl">https://doi.org/10.1016/j.chroma.2008.08.106</mods:identifier>
   <mods:abstract>We present a novel procedure for affinity partitioning of recombinant proteins fused to the choline-binding module C-LytA in aqueous two-phase systems containing poly(ethylene glycol) (PEG). Proteins tagged with the C-LytA module and exposed to the two-phase systems are quantitatively localized in the PEG-rich phase, whereas subsequent addition of the natural ligand choline specifically shifts their localization to the PEG-poor phase by displacement of the polymer from the binding sites. The described procedure is simple, scalable and reproducible, and has been successfully applied to the purification of four diverse proteins, resulting in high yields and purity.</mods:abstract>
   <mods:language>
      <mods:languageTerm>eng</mods:languageTerm>
   </mods:language>
   <mods:accessCondition type="useAndReproduction">http://creativecommons.org/licenses/by/4.0/</mods:accessCondition>
   <mods:accessCondition type="useAndReproduction">open access</mods:accessCondition>
   <mods:accessCondition type="useAndReproduction">Attribution 4.0 International</mods:accessCondition>
   <mods:titleInfo>
      <mods:title>Affinity partitioning of proteins tagged with choline-binding modules in aqueous two-phase systems</mods:title>
   </mods:titleInfo>
   <mods:genre>journal article</mods:genre>
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