| pubmed-article:10361002 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10361002 | lifeskim:mentions | umls-concept:C0680730 | lld:lifeskim |
| pubmed-article:10361002 | lifeskim:mentions | umls-concept:C1511790 | lld:lifeskim |
| pubmed-article:10361002 | lifeskim:mentions | umls-concept:C2267219 | lld:lifeskim |
| pubmed-article:10361002 | lifeskim:mentions | umls-concept:C0016315 | lld:lifeskim |
| pubmed-article:10361002 | lifeskim:mentions | umls-concept:C0201699 | lld:lifeskim |
| pubmed-article:10361002 | lifeskim:mentions | umls-concept:C1148554 | lld:lifeskim |
| pubmed-article:10361002 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10361002 | pubmed:dateCreated | 1999-8-13 | lld:pubmed |
| pubmed-article:10361002 | pubmed:abstractText | We have developed a nonradioactive method to assay UDP-Gal:beta-d-GlcNAcbeta1,4-galactosyltransferase (beta4GalT-I) enzymatic activity. Capillary electrophoresis combined with laser-induced fluorescence detection (CE-LIF) was employed to provide a baseline separation of FITC-conjugated O-GlcNAc-containing substrate peptides and galactose-capped product peptides, while at the same time allowing a level of detection in the low attomole range (10(-18)). The addition of 2 mM hexamethylene diamine to the borate-based capillary electrophoretic buffer modulated the electroosmotic flow, resulting in optimum separation of the glycopeptide product from reactant. beta4GalT-I activity was dependent upon the addition of both manganese and UDP-galactose. Using this assay, we show that two beta4GalT-I constructs, predicted to localize to different intracellular compartments, are enzymatically active when expressed in vitro using a rabbit reticulocyte transcription-translation system. The high sensitivity of product detection by CE-LIF in combination with in vitro transcription-translation is applicable to the facile determination of the enzymatic activity of other newly cloned glycosyltransferases. | lld:pubmed |
| pubmed-article:10361002 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10361002 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10361002 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10361002 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10361002 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10361002 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10361002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10361002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10361002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10361002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10361002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10361002 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10361002 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10361002 | pubmed:issn | 0003-2697 | lld:pubmed |
| pubmed-article:10361002 | pubmed:author | pubmed-author:ShaperJ HJH | lld:pubmed |
| pubmed-article:10361002 | pubmed:author | pubmed-author:HartG WGW | lld:pubmed |
| pubmed-article:10361002 | pubmed:author | pubmed-author:SujaJ AJA | lld:pubmed |
| pubmed-article:10361002 | pubmed:author | pubmed-author:ShaperN LNL | lld:pubmed |
| pubmed-article:10361002 | pubmed:copyrightInfo | Copyright 1999 Academic Press. | lld:pubmed |
| pubmed-article:10361002 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10361002 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10361002 | pubmed:volume | 271 | lld:pubmed |
| pubmed-article:10361002 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10361002 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10361002 | pubmed:pagination | 36-42 | lld:pubmed |
| pubmed-article:10361002 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10361002 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10361002 | pubmed:articleTitle | Determination of beta1,4-galactosyltransferase enzymatic activity by capillary electrophoresis and laser-induced fluorescence detection. | lld:pubmed |
| pubmed-article:10361002 | pubmed:affiliation | School of Medicine, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21207, USA. | lld:pubmed |
| pubmed-article:10361002 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10361002 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:10361002 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
