| pubmed-article:7575605 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7575605 | lifeskim:mentions | umls-concept:C0699040 | lld:lifeskim |
| pubmed-article:7575605 | lifeskim:mentions | umls-concept:C0032594 | lld:lifeskim |
| pubmed-article:7575605 | lifeskim:mentions | umls-concept:C0016263 | lld:lifeskim |
| pubmed-article:7575605 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:7575605 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:7575605 | pubmed:dateCreated | 1995-11-9 | lld:pubmed |
| pubmed-article:7575605 | pubmed:abstractText | Cell surface expressed lactosaminyl glycans were determined on live cells by flow cytometry using a sialyltransferase mediated labeling procedure. Fluorescent CMP-sialic acid and Gal beta 1,4GlcNAc alpha 2,6-sialyltransferase were applied to probe expression of acceptor glycans on untreated or sialidase pretreated erythrocytes. After enzymatic fluorescence labeling, erythrocytes were treated with endo-beta-galactosidase or trypsin to distinguish polylactosaminyl- and complex-type glycans. The expression of lactosaminyl sequences on cord- was 20% lower than on adult cells. After sialidase treatment fluorescence incorporation on both cell types increased twofold compared to untreated cells indicating a low sialylation extent. A recombinant alpha 2,3-sialyltransferase was preferentially labeling polylactosaminyl glycans. Taking advantage of the different fine specificity as determined here, alpha 2,6- and alpha 2,3-sialyltransferase can be applied to distinguish certain types of lactosaminyl glycans. | lld:pubmed |
| pubmed-article:7575605 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7575605 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7575605 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7575605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7575605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7575605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7575605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7575605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7575605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7575605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7575605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7575605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7575605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7575605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7575605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7575605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7575605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7575605 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7575605 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:7575605 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:7575605 | pubmed:author | pubmed-author:GrossH JHJ | lld:pubmed |
| pubmed-article:7575605 | pubmed:author | pubmed-author:Schwartz-Albi... | lld:pubmed |
| pubmed-article:7575605 | pubmed:author | pubmed-author:SauerAA | lld:pubmed |
| pubmed-article:7575605 | pubmed:author | pubmed-author:BollheimerL... | lld:pubmed |
| pubmed-article:7575605 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7575605 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:7575605 | pubmed:volume | 215 | lld:pubmed |
| pubmed-article:7575605 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7575605 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7575605 | pubmed:pagination | 30-40 | lld:pubmed |
| pubmed-article:7575605 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:7575605 | pubmed:meshHeading | pubmed-meshheading:7575605-... | lld:pubmed |
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| pubmed-article:7575605 | pubmed:meshHeading | pubmed-meshheading:7575605-... | lld:pubmed |
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| pubmed-article:7575605 | pubmed:meshHeading | pubmed-meshheading:7575605-... | lld:pubmed |
| pubmed-article:7575605 | pubmed:meshHeading | pubmed-meshheading:7575605-... | lld:pubmed |
| pubmed-article:7575605 | pubmed:meshHeading | pubmed-meshheading:7575605-... | lld:pubmed |
| pubmed-article:7575605 | pubmed:meshHeading | pubmed-meshheading:7575605-... | lld:pubmed |
| pubmed-article:7575605 | pubmed:meshHeading | pubmed-meshheading:7575605-... | lld:pubmed |
| pubmed-article:7575605 | pubmed:meshHeading | pubmed-meshheading:7575605-... | lld:pubmed |
| pubmed-article:7575605 | pubmed:meshHeading | pubmed-meshheading:7575605-... | lld:pubmed |
| pubmed-article:7575605 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7575605 | pubmed:articleTitle | Enzymatic analysis of cell surface lactosaminyl glycans by flow cytometry. | lld:pubmed |
| pubmed-article:7575605 | pubmed:affiliation | Institut f?r Biochemie II, Universität Heidelberg, FRG. | lld:pubmed |
| pubmed-article:7575605 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7575605 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
