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Analysis of glycopeptide antibiotics using micellar electrokinetic chromatography and borate complexation
Micellar electrokinetic chromatography (MEKC) was investigated as a technique for the separation and analysis of the following related glycopeptide antibiotics: α‐avoparcin, β‐avoparcin, ristocetin A, ristocetin B and vancomycin. Sodium dodecyl sulfate (SDS) micelles were employed as the pseudostati...
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Published in: | Biomedical chromatography 2003-03, Vol.17 (2-3), p.172-181 |
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container_title | Biomedical chromatography |
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creator | Lucas, Carmelle Foley, Joe P. Ahuja, Eric S. |
description | Micellar electrokinetic chromatography (MEKC) was investigated as a technique for the separation and analysis of the following related glycopeptide antibiotics: α‐avoparcin, β‐avoparcin, ristocetin A, ristocetin B and vancomycin. Sodium dodecyl sulfate (SDS) micelles were employed as the pseudostationary phase in conjunction with borate or CHES buffers at pH 9.2. A complete separation of the glycopeptides was achieved only when two separation mechanisms were employed simultaneously: (i) differential partitioning of the glycopeptides into SDS micelles; and (ii) differential complexation of the glycopeptides with the borate anion from the borate buffer. Quantitatively, linearity was confirmed for each antibiotic from 0.5 to 40 ppm, with correlation coefficients (r2) ranging from 0.9996 (vancomycin and β‐avoparcin) to 0.9986 (α‐avoparcin). Detection limits ranging from 0.01 ppm (vancomycin) to 0.2 ppm (avoparcin) were achieved, and the mean recovery of avoparcin at the 10 ppm level was 99.2%. Copyright © 2003 John Wiley & Sons, Ltd. |
doi_str_mv | 10.1002/bmc.235 |
format | article |
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Sodium dodecyl sulfate (SDS) micelles were employed as the pseudostationary phase in conjunction with borate or CHES buffers at pH 9.2. A complete separation of the glycopeptides was achieved only when two separation mechanisms were employed simultaneously: (i) differential partitioning of the glycopeptides into SDS micelles; and (ii) differential complexation of the glycopeptides with the borate anion from the borate buffer. Quantitatively, linearity was confirmed for each antibiotic from 0.5 to 40 ppm, with correlation coefficients (r2) ranging from 0.9996 (vancomycin and β‐avoparcin) to 0.9986 (α‐avoparcin). Detection limits ranging from 0.01 ppm (vancomycin) to 0.2 ppm (avoparcin) were achieved, and the mean recovery of avoparcin at the 10 ppm level was 99.2%. Copyright © 2003 John Wiley & Sons, Ltd.</description><identifier>ISSN: 0269-3879</identifier><identifier>EISSN: 1099-0801</identifier><identifier>DOI: 10.1002/bmc.235</identifier><identifier>PMID: 12717807</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Anti-Bacterial Agents - analysis ; avoparcin ; borate complexation ; Borates - chemistry ; Buffers ; capillary electrophoresis (CE) ; Chromatography, Micellar Electrokinetic Capillary - methods ; glycopeptide antibiotics ; Glycopeptides ; Hydrogen-Ion Concentration ; micellar electrokinetic chromatography (MEKC) ; Osmolar Concentration ; Stereoisomerism ; vancomycin</subject><ispartof>Biomedical chromatography, 2003-03, Vol.17 (2-3), p.172-181</ispartof><rights>Copyright © 2003 John Wiley & Sons, Ltd.</rights><rights>Copyright 2003 John Wiley & Sons, Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4075-a286529d0465aa551662e8c45020256b4be554dab134f8ab8baa5aa47b54d8143</citedby><cites>FETCH-LOGICAL-c4075-a286529d0465aa551662e8c45020256b4be554dab134f8ab8baa5aa47b54d8143</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12717807$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lucas, Carmelle</creatorcontrib><creatorcontrib>Foley, Joe P.</creatorcontrib><creatorcontrib>Ahuja, Eric S.</creatorcontrib><title>Analysis of glycopeptide antibiotics using micellar electrokinetic chromatography and borate complexation</title><title>Biomedical chromatography</title><addtitle>Biomed. Chromatogr</addtitle><description>Micellar electrokinetic chromatography (MEKC) was investigated as a technique for the separation and analysis of the following related glycopeptide antibiotics: α‐avoparcin, β‐avoparcin, ristocetin A, ristocetin B and vancomycin. Sodium dodecyl sulfate (SDS) micelles were employed as the pseudostationary phase in conjunction with borate or CHES buffers at pH 9.2. A complete separation of the glycopeptides was achieved only when two separation mechanisms were employed simultaneously: (i) differential partitioning of the glycopeptides into SDS micelles; and (ii) differential complexation of the glycopeptides with the borate anion from the borate buffer. Quantitatively, linearity was confirmed for each antibiotic from 0.5 to 40 ppm, with correlation coefficients (r2) ranging from 0.9996 (vancomycin and β‐avoparcin) to 0.9986 (α‐avoparcin). Detection limits ranging from 0.01 ppm (vancomycin) to 0.2 ppm (avoparcin) were achieved, and the mean recovery of avoparcin at the 10 ppm level was 99.2%. Copyright © 2003 John Wiley & Sons, Ltd.</description><subject>Anti-Bacterial Agents - analysis</subject><subject>avoparcin</subject><subject>borate complexation</subject><subject>Borates - chemistry</subject><subject>Buffers</subject><subject>capillary electrophoresis (CE)</subject><subject>Chromatography, Micellar Electrokinetic Capillary - methods</subject><subject>glycopeptide antibiotics</subject><subject>Glycopeptides</subject><subject>Hydrogen-Ion Concentration</subject><subject>micellar electrokinetic chromatography (MEKC)</subject><subject>Osmolar Concentration</subject><subject>Stereoisomerism</subject><subject>vancomycin</subject><issn>0269-3879</issn><issn>1099-0801</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><recordid>eNqFkE1v1DAQhi0EoktB_APkExyqlLEdf-RYIlpApRwAcbRsx7s1TeLU9orm35M2KzghTiPNPO-j0YvQSwKnBIC-tYM7pYw_QhsCTVOBAvIYbYCKpmJKNkfoWc4_AaARVD5FR4RKIhXIDQpno-nnHDKOW7zrZxcnP5XQeWzGEmyIJbiM9zmMOzwE5_veJOx770qKN2H0yxm76xQHU-Iumel6XoIdtjGZ4rGLw9T7O1NCHJ-jJ1vTZ__iMI_R9_P339oP1eWXi4_t2WXlapC8MlQJTpsOasGN4ZwIQb1yNQcKlAtbW8953RlLWL1Vxiq7UMbU0i5bRWp2jF6v3inF273PRQ8hPzw--rjPWjJKgTH-X5AoSTlV98Y3K-hSzDn5rZ5SGEyaNQF9X79e6tf0QfnqoNzbwXd_uUPfC3CyAr9C7-d_efS7z-2qq1Y65OLv_tAm3WghmeT6x9WFJuSqFbL9pL-y358Wnlw</recordid><startdate>200303</startdate><enddate>200303</enddate><creator>Lucas, Carmelle</creator><creator>Foley, Joe P.</creator><creator>Ahuja, Eric S.</creator><general>John Wiley & Sons, Ltd</general><scope>BSCLL</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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>200303</creationdate><title>Analysis of glycopeptide antibiotics using micellar electrokinetic chromatography and borate complexation</title><author>Lucas, Carmelle ; Foley, Joe P. ; Ahuja, Eric S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4075-a286529d0465aa551662e8c45020256b4be554dab134f8ab8baa5aa47b54d8143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Anti-Bacterial Agents - analysis</topic><topic>avoparcin</topic><topic>borate complexation</topic><topic>Borates - chemistry</topic><topic>Buffers</topic><topic>capillary electrophoresis (CE)</topic><topic>Chromatography, Micellar Electrokinetic Capillary - methods</topic><topic>glycopeptide antibiotics</topic><topic>Glycopeptides</topic><topic>Hydrogen-Ion Concentration</topic><topic>micellar electrokinetic chromatography (MEKC)</topic><topic>Osmolar Concentration</topic><topic>Stereoisomerism</topic><topic>vancomycin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lucas, Carmelle</creatorcontrib><creatorcontrib>Foley, Joe P.</creatorcontrib><creatorcontrib>Ahuja, Eric S.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biomedical chromatography</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lucas, Carmelle</au><au>Foley, Joe P.</au><au>Ahuja, Eric S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of glycopeptide antibiotics using micellar electrokinetic chromatography and borate complexation</atitle><jtitle>Biomedical chromatography</jtitle><addtitle>Biomed. Chromatogr</addtitle><date>2003-03</date><risdate>2003</risdate><volume>17</volume><issue>2-3</issue><spage>172</spage><epage>181</epage><pages>172-181</pages><issn>0269-3879</issn><eissn>1099-0801</eissn><abstract>Micellar electrokinetic chromatography (MEKC) was investigated as a technique for the separation and analysis of the following related glycopeptide antibiotics: α‐avoparcin, β‐avoparcin, ristocetin A, ristocetin B and vancomycin. Sodium dodecyl sulfate (SDS) micelles were employed as the pseudostationary phase in conjunction with borate or CHES buffers at pH 9.2. A complete separation of the glycopeptides was achieved only when two separation mechanisms were employed simultaneously: (i) differential partitioning of the glycopeptides into SDS micelles; and (ii) differential complexation of the glycopeptides with the borate anion from the borate buffer. Quantitatively, linearity was confirmed for each antibiotic from 0.5 to 40 ppm, with correlation coefficients (r2) ranging from 0.9996 (vancomycin and β‐avoparcin) to 0.9986 (α‐avoparcin). Detection limits ranging from 0.01 ppm (vancomycin) to 0.2 ppm (avoparcin) were achieved, and the mean recovery of avoparcin at the 10 ppm level was 99.2%. Copyright © 2003 John Wiley & Sons, Ltd.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>12717807</pmid><doi>10.1002/bmc.235</doi><tpages>10</tpages></addata></record> |
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subjects | Anti-Bacterial Agents - analysis avoparcin borate complexation Borates - chemistry Buffers capillary electrophoresis (CE) Chromatography, Micellar Electrokinetic Capillary - methods glycopeptide antibiotics Glycopeptides Hydrogen-Ion Concentration micellar electrokinetic chromatography (MEKC) Osmolar Concentration Stereoisomerism vancomycin |
title | Analysis of glycopeptide antibiotics using micellar electrokinetic chromatography and borate complexation |
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