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Consejo Nacional de Ciencia y Tecnología, CONACYT: 165730
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National Science Foundation, NSF: MCB-9726721
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Generically Dependent Continuant
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individual
rights: termsOfUse
date: 2026-08-28T03:00:15
publisher: vivo
type: Document
label: RDF description of Adsorption of peptides and small proteins with control access polymer permeation to affinity binding sites. Part II: Polymer permeation-ion exchange separation adsorbents with polyethylene glycol and strong anion exchange groups - http://orbis.uaslp.mx/vivo/individual/scopus3259

Article
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scopus3259
related by: authorship_18923
chemicalscas: agarose, 9012-36-6; chloride, 16887-00-6; insulin, 9004-10-8; macrogol, 25322-68-3; trimethylammonium salt derivative, 16962-53-1; Anions; Insulin; Polyethylene Glycols; Polymers; Proteins
has funding vehicle: University of Arizona, UA
doi: 10.1016/j.chroma.2011.12.092
type: Generically Dependent Continuant
pmid: 22265175
page end: 137
has publication venue: Journal of Chromatography A
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volume: 1227
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has funding vehicle: Consejo Nacional de Ciencia y Tecnología, CONACYT: 165730
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most specific type: Document
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date time value: article date 3260
related by: authorship_18922
has funding vehicle: National Science Foundation, NSF: MCB-9726721
page start: 126
label: Adsorption of peptides and small proteins with control access polymer permeation to affinity binding sites. Part II: Polymer permeation-ion exchange separation adsorbents with polyethylene glycol and strong anion exchange groups
abstract: In chromatographic separations, the most general problem in small biomolecule isolation and purification is that such biomolecules are usually found in extremely low concentrations together with high concentrations of large molecular weight proteins. In the first part of this work, adsorption and size exclusion chromatography (AdSEC) controlled access media, using polyethylene glycol (PEG) as a semi-permeable barrier on a polysaccharide Immobilized Metal Affinity Chromatography (IMAC) matrix was synthesized and used to develop chromatographic adsorbents that preferentially adsorb and separate low molecular weight biomolecules while rejecting large molecular weight proteins. In this second part, we expand the concept of controlled access polymer permeation adsorption (CAPPA) media by grafting polyethylene glycol (PEG) on a high capacity polysaccharide ion exchange (IEX) chromatographic resin where PEG acts as a semi-permeable barrier that preferentially allows the permeation of small molecules while rejecting large ones. The IEX resin bearing quaternary ammonium groups binds permeated biomolecules according to their ion exchange affinity while excluding large biomolecules by the PEG barrier and thus cannot compete for the binding sites. This new AdSEC media was used to study the retention of peptides and proteins covering a wide range of molecular weights from 1 to 150. kDa. The effect of protein molecular weight towards retention by ion exchange was performed using pure protein solutions. Recovery of insulin from insulin-spiked human serum and insulin-spiked human urine was evaluated under polymer controlled permeation conditions. The CAPPA media consisted of agarose beads modified with amino-PEG-methoxy and with trimethyl ammonium groups, having chloride capacities between 20 and 40. μeq/mL and were effective in rejecting high molecular weight proteins while allowing the preferential adsorption of small proteins and peptides. © 2012 Elsevier B.V.
freetext keyword: Adsorption chromatography; Bioseparations; Ion exchange chromatography; Non-fouling surface; Polyethylene glycol; RAM Adsorption chromatography; Affinity binding; Agarose beads; Ammonium groups; Bio separation; Chloride capacity; Chromatographic resins; Chromatographic separations; Control access; High capacity; High concentration; High molecular weight protein; Human serum; Human urine; Immobilized metal affinity chromatography; Ion exchange chromatography; Isolation and purification; Large biomolecules; Low concentrations; Low molecular weight; matrix; Nonfouling surfaces; Preferential adsorption; Protein solution; Quaternary ammonium group; Small molecules; Strong anion exchanges; Trimethyl; Access control; Adsorption; Affinity chromatography; Ammonium compounds; Biomolecules; Biosynthesis; Body fluids; Chlorine compounds; Chromatographic analysis; Insulin; Ion exchange; Liquid chromatography; Molecular weight; Peptides; Polyethylene oxides; Polymers; Random access storage; Resins; Separation; Polyethylene glycols; adsorbent; agarose; chloride; insulin; macrogol; polymer; quaternary ammonium derivative; resin; trimethylammonium salt derivative; adsorption chromatography; adsorption kinetics; anion exchange; article; binding affinity; binding site; bioseparation; concentration (parameters); controlled study; gel permeation chromatography; human; immobilized metal affinity chromatography; ion exchange chromatography; molecular weight; priority journal; protein isolation; protein purification; Adsorption; Animals; Anions; Chromatography, Ion Exchange; Humans; Insulin; Models, Chemical; Molecular Weight; Polyethylene Glycols; Polymers; Proteins
related by: authorship_18921
estado: published
crisid: 3260
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Information Content Entity
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Journal of Chromatography A
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University of Arizona, UA
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funding vehicle for: scopus3259