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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1988-6-14
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pubmed:abstractText |
Concanavalin A (Con A) was immobilized via metal interactions on macroporous, microparticulate silica support having covalently bound iminodiacetic acid functions (IDA-silica) chelated with Cu(II) at the surface. The amount of copper and of Con A in the column could readily be controlled by the conditions used for chelating the metal by IDA-silica and for immobilization of the lectin. The retention behavior of columns packed with the stationary phase did not change under a wide range of elution conditions, indicating no loss of immobilized lectin. However, the Con A proper could readily be removed from the column at pH 3.0 or together with Cu(II) by perfusion with EDTA at neutral pH. Columns containing Con A immobilized by this technique exhibited dual retention behavior for proteins, glycoproteins, and carbohydrates according to the pertinent glycan-lectin or protein-metal interactions. The glycoproteins, peroxidase and alpha 1-acid glycoprotein, were retained by the Con A moiety and eluted with eluents containing competing sugars, whereas the proteins, beta-lactoglobulin, alpha-chymotrypsinogen A, and ribonuclease A and B were retained by the chelated copper and were eluted and separated with eluents containing sodium chloride or borate. Binding constants of glycosides on the immobilized Con A were evaluated chromatographically and found to be one-third to two-thirds those reported in the literature on the basis of experiments in free solution.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrates,
http://linkedlifedata.com/resource/pubmed/chemical/Concanavalin A,
http://linkedlifedata.com/resource/pubmed/chemical/Copper,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Imino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Silicon Dioxide,
http://linkedlifedata.com/resource/pubmed/chemical/iminodiacetic acid
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0003-2697
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
169
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
172-80
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2835917-Carbohydrates,
pubmed-meshheading:2835917-Chromatography, Affinity,
pubmed-meshheading:2835917-Chromatography, High Pressure Liquid,
pubmed-meshheading:2835917-Concanavalin A,
pubmed-meshheading:2835917-Copper,
pubmed-meshheading:2835917-Glycoproteins,
pubmed-meshheading:2835917-Imino Acids,
pubmed-meshheading:2835917-Kinetics,
pubmed-meshheading:2835917-Proteins,
pubmed-meshheading:2835917-Silicon Dioxide
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pubmed:year |
1988
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pubmed:articleTitle |
High-performance liquid chromatography with concanavalin A immobilized by metal interactions on the stationary phase.
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pubmed:affiliation |
Department of Chemical Engineering, Yale University, New Haven, Connecticut 06520.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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