| pubmed-article:8127069 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8127069 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:8127069 | lifeskim:mentions | umls-concept:C0026706 | lld:lifeskim |
| pubmed-article:8127069 | lifeskim:mentions | umls-concept:C0086650 | lld:lifeskim |
| pubmed-article:8127069 | lifeskim:mentions | umls-concept:C0011900 | lld:lifeskim |
| pubmed-article:8127069 | lifeskim:mentions | umls-concept:C2717977 | lld:lifeskim |
| pubmed-article:8127069 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:8127069 | pubmed:dateCreated | 1994-4-11 | lld:pubmed |
| pubmed-article:8127069 | pubmed:abstractText | 4-Methylumbelliferyl-alpha-N-acetylglucosamine 6-sulphate was synthesized and shown to be a substrate for the lysosomal N-acetylglucosamine-6-sulphate sulphatase (GlcNAc-6S sulphatase). Fibroblasts and leukocytes from 3 different Sanfilippo D patients showed < 1% of mean normal GlcNAc-6S sulphatase activity. The enzymatic liberation of the fluorochrome from 4-methyl-umbelliferyl-alpha-N-acetylglucosamine 6-sulphate requires the sequential action of the GlcNAc-6S sulphatase and alpha-N-acetylglucosaminidase. A normal level of alpha-N-acetylglucosaminidase activity was insufficient to complete the hydrolysis of the reaction intermediate 4-methylumbelliferyl-alpha-N-acetylglucosaminide formed by the GlcNAc-6S sulphatase. A second incubation in the presence of excess alpha-N-acetylglucosaminidase is needed to avoid underestimation of the GlcNAc-6S sulphatase activity. | lld:pubmed |
| pubmed-article:8127069 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8127069 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8127069 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8127069 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8127069 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8127069 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8127069 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8127069 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8127069 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8127069 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8127069 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8127069 | pubmed:issn | 0141-8955 | lld:pubmed |
| pubmed-article:8127069 | pubmed:author | pubmed-author:HOMM | lld:pubmed |
| pubmed-article:8127069 | pubmed:author | pubmed-author:KleijerW JWJ | lld:pubmed |
| pubmed-article:8127069 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:8127069 | pubmed:author | pubmed-author:Voznyi YaV | lld:pubmed |
| pubmed-article:8127069 | pubmed:author | pubmed-author:BoerA MAM | lld:pubmed |
| pubmed-article:8127069 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8127069 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:8127069 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8127069 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8127069 | pubmed:pagination | 935-41 | lld:pubmed |
| pubmed-article:8127069 | pubmed:dateRevised | 2007-3-21 | lld:pubmed |
| pubmed-article:8127069 | pubmed:meshHeading | pubmed-meshheading:8127069-... | lld:pubmed |
| pubmed-article:8127069 | pubmed:meshHeading | pubmed-meshheading:8127069-... | lld:pubmed |
| pubmed-article:8127069 | pubmed:meshHeading | pubmed-meshheading:8127069-... | lld:pubmed |
| pubmed-article:8127069 | pubmed:meshHeading | pubmed-meshheading:8127069-... | lld:pubmed |
| pubmed-article:8127069 | pubmed:meshHeading | pubmed-meshheading:8127069-... | lld:pubmed |
| pubmed-article:8127069 | pubmed:meshHeading | pubmed-meshheading:8127069-... | lld:pubmed |
| pubmed-article:8127069 | pubmed:meshHeading | pubmed-meshheading:8127069-... | lld:pubmed |
| pubmed-article:8127069 | pubmed:meshHeading | pubmed-meshheading:8127069-... | lld:pubmed |
| pubmed-article:8127069 | pubmed:meshHeading | pubmed-meshheading:8127069-... | lld:pubmed |
| pubmed-article:8127069 | pubmed:meshHeading | pubmed-meshheading:8127069-... | lld:pubmed |
| pubmed-article:8127069 | pubmed:meshHeading | pubmed-meshheading:8127069-... | lld:pubmed |
| pubmed-article:8127069 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8127069 | pubmed:articleTitle | A fluorimetric enzyme assay for the diagnosis of Sanfilippo disease type D (MPS IIID). | lld:pubmed |
| pubmed-article:8127069 | pubmed:affiliation | Department of Clinical Genetics, Erasmus University, Rotterdam, The Netherlands. | lld:pubmed |
| pubmed-article:8127069 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8127069 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8127069 | lld:pubmed |
