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dc.contributor.authorLee, K.B.
dc.contributor.authorDesai, U.R.
dc.contributor.authorPalcic, M.M.
dc.contributor.authorHindsgaul, O.
dc.contributor.authorLinhardt, Robert J.
dc.date1992
dc.date.accessioned2022-06-27T17:14:57Z
dc.date.available2022-06-27T17:14:57Z
dc.date.issued1992-08-15
dc.identifier.citationAn Electrophoresis-Based Assay For Glycosyltransferase Activity, K.B. Lee, U.R. Desai, M.M. Palcic, O. Hindsgaul, R.J. Linhardt, Analytical Biochemistry, 205, 108-114 (1992).
dc.identifier.issn10960309
dc.identifier.issn32697
dc.identifier.urihttps://doi.org/10.1016/0003-2697(92)90586-V
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5989
dc.descriptionAnalytical Biochemistry, 205, 108-114
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractPolyacrylamide gel electrophoresis (PAGE) and capillary zone electrophoresis (CZE) were used to measure the activity of glycosyltransferases. Acceptor molecules were prepared by reductive amination of the monopotassium 7-amino-1,3-naphthalenedisulfonic acid (AGA) Schiff base with sugars. The resulting sugar conjugates were purified by gradient PAGE and recovered using semidry electrotransfer into a positively charged nylon membrane. The beta(1----4)galactosyltransferase was shown, by PAGE analysis, to transfer a beta-galactosyl residue to the AGA conjugate of beta-D-GlcNAc-(1----4)-beta-D-GlcNAc-(1----4)-D-GlcNAc (compound 4). Similarly, alpha(1----2)fucosyltransferase isolated from porcine submaxillary glands was shown to transfer fucose from GDP-fucose to the AGA conjugate of beta-D-Gal-(1----4)-beta-D-GlcNAc-(1----6)-D-Gal (compound 5). This conjugate (compound 5) was also an acceptor for the alpha(1----3/4)fucosyltransferase partially purified from human milk. The latter reaction was followed by both gradient PAGE and CZE, having sensitivities of 200 pmol and 80 fmol, respectively.
dc.description.sponsorshipNational Institutes of Health
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/0003-2697(92)90586-V
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofAnalytical Biochemistry
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleAn Electrophoresis-Based Assay For Glycosyltransferase Activity
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/0003-2697(92)90586-V
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dcterms.isVersionOfhttps://doi.org/10.1016/0003-2697(92)90586-V
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dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages108-114
rpi.description.volume205


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