| pubmed-article:8412007 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8412007 | lifeskim:mentions | umls-concept:C0026706 | lld:lifeskim |
| pubmed-article:8412007 | lifeskim:mentions | umls-concept:C0086649 | lld:lifeskim |
| pubmed-article:8412007 | lifeskim:mentions | umls-concept:C0011900 | lld:lifeskim |
| pubmed-article:8412007 | lifeskim:mentions | umls-concept:C2717977 | lld:lifeskim |
| pubmed-article:8412007 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8412007 | pubmed:dateCreated | 1993-10-25 | lld:pubmed |
| pubmed-article:8412007 | pubmed:abstractText | Both the alpha- and beta-anomers of 4-methylumbelliferyl-D-glucosaminide were synthesized and shown to be substrates for the lysosomal acetyl-CoA:glucosaminide N-acetyltransferase. Using the beta-anomer, fibroblasts and leukocytes from 11 different Sanfilippo C patients showed < 1% of mean normal N-acetyltransferase activity. Heterozygotes showed intermediate activities. The enzymatic liberation of the fluorochrome from 4-methylumbelliferyl-beta-D-glucosaminide requires the sequential action of the N-acetyltransferase and beta-hexosaminidase. Normal beta-hexosaminidase activity caused complete hydrolysis of the reaction intermediate 4-methylumbelliferyl-beta-D-N-acetylglucosaminide formed by the N-acetyltransferase. In cell extracts with a beta-hexosaminidase deficiency, however, a second incubation in the presence of excess beta-hexosaminidase is needed to avoid underestimation of the N-acetyltransferase activity. | lld:pubmed |
| pubmed-article:8412007 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8412007 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8412007 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8412007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8412007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8412007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8412007 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8412007 | pubmed:issn | 0141-8955 | lld:pubmed |
| pubmed-article:8412007 | pubmed:author | pubmed-author:TsvetkovaI... | lld:pubmed |
| pubmed-article:8412007 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:8412007 | pubmed:author | pubmed-author:JanseH CHC | lld:pubmed |
| pubmed-article:8412007 | pubmed:author | pubmed-author:KarpovaE AEA | lld:pubmed |
| pubmed-article:8412007 | pubmed:author | pubmed-author:Voznyi YaV | lld:pubmed |
| pubmed-article:8412007 | pubmed:author | pubmed-author:DudukinaT VTV | lld:pubmed |
| pubmed-article:8412007 | pubmed:author | pubmed-author:BoerA MAM | lld:pubmed |
| pubmed-article:8412007 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8412007 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:8412007 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8412007 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8412007 | pubmed:pagination | 465-72 | lld:pubmed |
| pubmed-article:8412007 | pubmed:dateRevised | 2007-3-21 | lld:pubmed |
| pubmed-article:8412007 | pubmed:meshHeading | pubmed-meshheading:8412007-... | lld:pubmed |
| pubmed-article:8412007 | pubmed:meshHeading | pubmed-meshheading:8412007-... | lld:pubmed |
| pubmed-article:8412007 | pubmed:meshHeading | pubmed-meshheading:8412007-... | lld:pubmed |
| pubmed-article:8412007 | pubmed:meshHeading | pubmed-meshheading:8412007-... | lld:pubmed |
| pubmed-article:8412007 | pubmed:meshHeading | pubmed-meshheading:8412007-... | lld:pubmed |
| pubmed-article:8412007 | pubmed:meshHeading | pubmed-meshheading:8412007-... | lld:pubmed |
| pubmed-article:8412007 | pubmed:meshHeading | pubmed-meshheading:8412007-... | lld:pubmed |
| pubmed-article:8412007 | pubmed:meshHeading | pubmed-meshheading:8412007-... | lld:pubmed |
| pubmed-article:8412007 | pubmed:meshHeading | pubmed-meshheading:8412007-... | lld:pubmed |
| pubmed-article:8412007 | pubmed:meshHeading | pubmed-meshheading:8412007-... | lld:pubmed |
| pubmed-article:8412007 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8412007 | pubmed:articleTitle | A fluorimetric enzyme assay for the diagnosis of Sanfilippo disease C (MPS III C). | lld:pubmed |
| pubmed-article:8412007 | pubmed:affiliation | Institute of Biochemistry, Academy of Sciences Armenian Republic, Yerevan. | lld:pubmed |
| pubmed-article:8412007 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8412007 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8412007 | lld:pubmed |
