dc.contributor.author | Lee, K.B. | |
dc.contributor.author | Desai, U.R. | |
dc.contributor.author | Palcic, M.M. | |
dc.contributor.author | Hindsgaul, O. | |
dc.contributor.author | Linhardt, Robert J. | |
dc.date | 1992 | |
dc.date.accessioned | 2022-06-27T17:14:57Z | |
dc.date.available | 2022-06-27T17:14:57Z | |
dc.date.issued | 1992-08-15 | |
dc.identifier.citation | An 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.issn | 10960309 | |
dc.identifier.issn | 32697 | |
dc.identifier.uri | https://doi.org/10.1016/0003-2697(92)90586-V | |
dc.identifier.uri | https://hdl.handle.net/20.500.13015/5989 | |
dc.description | Analytical Biochemistry, 205, 108-114 | |
dc.description | Note : 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.abstract | Polyacrylamide 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.sponsorship | National Institutes of Health | |
dc.description.uri | https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/0003-2697(92)90586-V | |
dc.language | en_US | |
dc.language.iso | ENG | |
dc.relation.ispartof | The Linhardt Research Labs Online Collection | |
dc.relation.ispartof | Rensselaer Polytechnic Institute, Troy, NY | |
dc.relation.ispartof | Analytical Biochemistry | |
dc.relation.uri | https://harc.rpi.edu/ | |
dc.subject | Biology | |
dc.subject | Chemistry and chemical biology | |
dc.subject | Chemical and biological engineering | |
dc.subject | Biomedical engineering | |
dc.title | An Electrophoresis-Based Assay For Glycosyltransferase Activity | |
dc.type | Article | |
dcterms.accessRights | https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/0003-2697(92)90586-V | |
dcterms.isPartOf | Journal | |
dcterms.isVersionOf | https://doi.org/10.1016/0003-2697(92)90586-V | |
dc.rights.holder | In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/ | |
dc.creator.identifier | https://orcid.org/0000-0003-2219-5833 | |
dc.relation.department | The Linhardt Research Labs. | |
dc.relation.department | The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS) | |
rpi.description.pages | 108-114 | |
rpi.description.volume | 205 | |