NDLI: Performance of hydrophobic interaction ligands for human membrane-bound catechol-O-methyltransferase purification

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Performance of hydrophobic interaction ligands for human membrane-bound catechol-O-methyltransferase purification

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Santos, Fátima Milhano Pedro, Augusto Quaresma Soares, Rui Filipe Martins, Rita Bonifácio, Maria João Queiroz, João António Passarinha, Luís António
Description	Country affiliation: Portugal Author Affiliation: Santos FM ( Centro de Investigação em Ciências da Saúde, Universidade da Beira Interior, Covilhã, Portugal.)
Abstract	Despite of membrane catechol-O-methyltransferase (MBCOMT, EC 2.1.1.6) physiological importance on catecholamines’ O-methylation, no studies allowed their total isolation. Therefore, for the first time, we compare the performance of three hydrophobic adsorbents (butyl-, epoxy-, and octyl-Sepharose) in purification of recombinant human COMT (hMBCOMT) from crude Brevibacillus choshinensis cell lysates to develop a sustainable chromatographic process. Hydrophobic matrices were evaluated in terms of selectivity and hMBCOMT's binding and elution conditions. Results show that hMBCOMT's adsorption was promoted on octyl and butyl at ≤375 mM $NaH_{2}PO_{4,}$ while on epoxy higher concentrations (>850 mM) were required. Additionally, hMBCOMT's elution was promoted on epoxy, butyl, and octyl using respectively 0.1–0.5, 0.25–1, and 1% of Triton X-100. On butyl media, a stepwise strategy using 375 and 0 mM $NaH_{2}PO_{4},$ followed by three elution steps at 0.25, 0.7 and 1% Triton X-100, allowed selective hMBCOMT isolation. In conclusion, significant amounts of MBCOMT were purified with high selectivity on a single chromatography procedure, despite its elution occurs on multiple peaks. Although successful applications of hydrophobic interaction chromatography in purification of membrane proteins are uncommon, we proved that traditional hydrophobic matrices can open a promising unexplored field to fulfill specific requirements for kinetic and pharmacological trials.
File Format	HTM / HTML
ISSN	16159306
Issue Number	11
Volume Number	36
e-ISSN	16159314
Journal	Journal of Separation Science
Language	English
Publisher	Wiley-VCH
Publisher Date	2013-06-01
Publisher Place	Germany
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Analytical Discipline Chemistry Catechol O-methyltransferase Isolation & Purification Chromatography, Liquid Methods Adsorption Brevibacillus Genetics Metabolism Chemistry Humans Hydrophobic And Hydrophilic Interactions Ligands Recombinant Proteins Evaluation Studies Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Analytical Chemistry Filtration and Separation

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