Hybrid affinity chromatography of α-galactosidase from Verbascum thapsus L
Purification of α-galactosidase from the roots of Verbascum thapsus L. was difficult to achieve using conventional methods due to the presence of coloured contaminants. A newly developed procedure, hybrid affinity chromatography, which was based on a mixed matrix separation procedure, using a substr...
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Veröffentlicht in: | Journal of Chromatography A 1998-05, Vol.808 (1), p.133-139 |
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container_title | Journal of Chromatography A |
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creator | Bom, Isaac van Wassenaar, Dick Boot, Johan |
description | Purification of α-galactosidase from the roots of
Verbascum thapsus L. was difficult to achieve using conventional methods due to the presence of coloured contaminants. A newly developed procedure, hybrid affinity chromatography, which was based on a mixed matrix separation procedure, using a substrate analogue and an immobilized metal affinity matrix as ligands, respectively, allowed the purification of this enzyme with good recovery. The method should be applicable to other proteins as well. |
doi_str_mv | 10.1016/S0021-9673(98)00104-6 |
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Verbascum thapsus L. was difficult to achieve using conventional methods due to the presence of coloured contaminants. A newly developed procedure, hybrid affinity chromatography, which was based on a mixed matrix separation procedure, using a substrate analogue and an immobilized metal affinity matrix as ligands, respectively, allowed the purification of this enzyme with good recovery. The method should be applicable to other proteins as well.</description><subject>alpha-Galactosidase - isolation & purification</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Chromatography, Affinity - methods</subject><subject>Concanavalin A</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Galactosidase</subject><subject>Hydrolases</subject><subject>Isoelectric Focusing</subject><subject>Isoelectric Point</subject><subject>Plant Lectins</subject><subject>Plant Roots - enzymology</subject><subject>Plants - enzymology</subject><issn>0021-9673</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtKxDAUhrNQdBx9hIEuRHRRTdI2bVYigzrigAsv23CaJjOR3kxaoY_li_hMZmbKbA0HAvm_c3L4EJoRfE0wYTevGFMScpZGlzy7wpjgOGQHaLJ_PkYnzn36IMUpPUJHnCWUkGSCnhdDbk0RgNamNt0QyLVtKuialYV2PQSNDn5_whWUILvGmQKcCrQngg9lc3Cyr4JuDa3rXbA8RYcaSqfOxnuK3h_u3-aLcPny-DS_W4YyyngX5mkMlMaS0yJVTFMMJFIpj4FDliRFEmmuc0jznLCYcxURwBz7ONP-xEUeTdHFbm5rm69euU5UxklVllCrpnci5dxXknkw2YHSNs5ZpUVrTQV2EASLjTixFSc2hgTPxFacYL5vNn7Q55Uq9l2jNZ-fj7k3AKW2UEvj9hiljNGIe-x2hykv49soK5w0qpaqMFbJThSN-WeRP-_ujVI</recordid><startdate>19980529</startdate><enddate>19980529</enddate><creator>Bom, Isaac</creator><creator>van Wassenaar, Dick</creator><creator>Boot, Johan</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19980529</creationdate><title>Hybrid affinity chromatography of α-galactosidase from Verbascum thapsus L</title><author>Bom, Isaac ; van Wassenaar, Dick ; Boot, Johan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-b74a224c92d7e6f20a13e794a9a855d53f9fba7bb16499e31a09094a8ffff4db3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>alpha-Galactosidase - isolation & purification</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Chromatography, Affinity - methods</topic><topic>Concanavalin A</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzymes</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Galactosidase</topic><topic>Hydrolases</topic><topic>Isoelectric Focusing</topic><topic>Isoelectric Point</topic><topic>Plant Lectins</topic><topic>Plant Roots - enzymology</topic><topic>Plants - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bom, Isaac</creatorcontrib><creatorcontrib>van Wassenaar, Dick</creatorcontrib><creatorcontrib>Boot, Johan</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of Chromatography A</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bom, Isaac</au><au>van Wassenaar, Dick</au><au>Boot, Johan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hybrid affinity chromatography of α-galactosidase from Verbascum thapsus L</atitle><jtitle>Journal of Chromatography A</jtitle><addtitle>J Chromatogr A</addtitle><date>1998-05-29</date><risdate>1998</risdate><volume>808</volume><issue>1</issue><spage>133</spage><epage>139</epage><pages>133-139</pages><issn>0021-9673</issn><coden>JOCRAM</coden><abstract>Purification of α-galactosidase from the roots of
Verbascum thapsus L. was difficult to achieve using conventional methods due to the presence of coloured contaminants. A newly developed procedure, hybrid affinity chromatography, which was based on a mixed matrix separation procedure, using a substrate analogue and an immobilized metal affinity matrix as ligands, respectively, allowed the purification of this enzyme with good recovery. The method should be applicable to other proteins as well.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>9652115</pmid><doi>10.1016/S0021-9673(98)00104-6</doi><tpages>7</tpages></addata></record> |
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subjects | alpha-Galactosidase - isolation & purification Analytical, structural and metabolic biochemistry Biological and medical sciences Chromatography, Affinity - methods Concanavalin A Electrophoresis, Polyacrylamide Gel Enzymes Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Galactosidase Hydrolases Isoelectric Focusing Isoelectric Point Plant Lectins Plant Roots - enzymology Plants - enzymology |
title | Hybrid affinity chromatography of α-galactosidase from Verbascum thapsus L |
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