Hdl Handle:
http://hdl.handle.net/10149/98817
Title:
Thiophilic nature of divinylsulphone cross-linked agarose
Authors:
Noel, R. J. (Richard); O'Hare, W. T. (Liam); Street, G. (Graham)
Affiliation:
University of Teesside. School of Science and Technology. Chemical and Biochemical Engineering Research Centre.
Citation:
Noel, R. J., O'Hare, W. T. and Street, G. (1996) 'Thiophilic nature of divinylsulphone cross-linked agarose', Journal of Chromatography A, 734 (2), pp.241-246.
Publisher:
Elsevier
Journal:
Journal of Chromatography A
Issue Date:
24-May-1996
URI:
http://hdl.handle.net/10149/98817
DOI:
10.1016/0021-9673(95)01313-X
Abstract:
We present data to suggest that divinylsulphone-activated matrix (DVS-gel) purifies immunoglobulins with the same protein-ligand interaction as the thiophilic ligand, T-gel. Divinylsulphone-activated matrix purifies IgG (> 90% pure) from blood serum with a binding capacity of 6.3 mg/ml, compared to 6.9 mg/ml with T-gel. It also separates IgG and sIgA from cheese whey, with the same dependency on water-structuring salt concentration as T-gel. We offer an explanation for these results in terms of the polymerisation of divinylsulphone and, therefore, offer a new structure for the so-called thiophilic ligand.
Type:
Article
Language:
en
Keywords:
agarose; divinylsulfone; immunoglobulins; stationary phases; LC; thiophilic interactions
ISSN:
0021-9673
Rights:
Author can archive post-print (ie final draft post-refereeing). For full details see http://www.sherpa.ac.uk/romeo/ [Accessed 14/05/2010]
Citation Count:
10 [Scopus, 14/05/2010]

Full metadata record

DC FieldValue Language
dc.contributor.authorNoel, R. J. (Richard)en
dc.contributor.authorO'Hare, W. T. (Liam)en
dc.contributor.authorStreet, G. (Graham)en
dc.date.accessioned2010-05-14T10:20:54Z-
dc.date.available2010-05-14T10:20:54Z-
dc.date.issued1996-05-24-
dc.identifier.citationJournal of Chromatography A; 734(2):241-246en
dc.identifier.issn0021-9673-
dc.identifier.doi10.1016/0021-9673(95)01313-X-
dc.identifier.urihttp://hdl.handle.net/10149/98817-
dc.description.abstractWe present data to suggest that divinylsulphone-activated matrix (DVS-gel) purifies immunoglobulins with the same protein-ligand interaction as the thiophilic ligand, T-gel. Divinylsulphone-activated matrix purifies IgG (> 90% pure) from blood serum with a binding capacity of 6.3 mg/ml, compared to 6.9 mg/ml with T-gel. It also separates IgG and sIgA from cheese whey, with the same dependency on water-structuring salt concentration as T-gel. We offer an explanation for these results in terms of the polymerisation of divinylsulphone and, therefore, offer a new structure for the so-called thiophilic ligand.en
dc.language.isoenen
dc.publisherElsevieren
dc.rightsAuthor can archive post-print (ie final draft post-refereeing). For full details see http://www.sherpa.ac.uk/romeo/ [Accessed 14/05/2010]en
dc.subjectagaroseen
dc.subjectdivinylsulfoneen
dc.subjectimmunoglobulinsen
dc.subjectstationary phasesen
dc.subjectLCen
dc.subjectthiophilic interactionsen
dc.titleThiophilic nature of divinylsulphone cross-linked agaroseen
dc.typeArticleen
dc.contributor.departmentUniversity of Teesside. School of Science and Technology. Chemical and Biochemical Engineering Research Centre.en
dc.identifier.journalJournal of Chromatography Aen
ref.citationcount10 [Scopus, 14/05/2010]en
or.citation.harvardNoel, R. J., O'Hare, W. T. and Street, G. (1996) 'Thiophilic nature of divinylsulphone cross-linked agarose', Journal of Chromatography A, 734 (2), pp.241-246.-
All Items in TeesRep are protected by copyright, with all rights reserved, unless otherwise indicated.