pubmed-article:7317006 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7317006 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
pubmed-article:7317006 | lifeskim:mentions | umls-concept:C0005270 | lld:lifeskim |
pubmed-article:7317006 | lifeskim:mentions | umls-concept:C0022173 | lld:lifeskim |
pubmed-article:7317006 | lifeskim:mentions | umls-concept:C1704711 | lld:lifeskim |
pubmed-article:7317006 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:7317006 | pubmed:dateCreated | 1982-2-12 | lld:pubmed |
pubmed-article:7317006 | pubmed:abstractText | A characteristic of the human lysosomal disorder I-cell disease is an abnormal excretion of most lysosomal hydrolases, including beta-N-acetyl-D-glucosaminidase (EC 3.2.1.30; beta-hexosaminidase) by cultured skin fibroblasts. Treatment of I-cell cultures with cycloheximide or tunicamycin demonstrated that (1) I-cell fibroblasts rapidly excrete all newly synthesized beta-hexosaminidase, (2) two qualitatively distinct pools of beta-hexosaminidase isoenzymes exist inside I-cell fibroblasts, one of which is a rapid-turnover excretory pool, and (3) the induction of an abnormal glycosylation of beta-hexosaminidase by tunicamycin in normal or I-cell fibroblast cultures does not affect subsequent excretion of the enzyme. | lld:pubmed |
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pubmed-article:7317006 | pubmed:language | eng | lld:pubmed |
pubmed-article:7317006 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7317006 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7317006 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:7317006 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7317006 | pubmed:month | Jun | lld:pubmed |
pubmed-article:7317006 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:7317006 | pubmed:author | pubmed-author:RattazziM CMC | lld:pubmed |
pubmed-article:7317006 | pubmed:author | pubmed-author:VladutiuG DGD | lld:pubmed |
pubmed-article:7317006 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7317006 | pubmed:day | 15 | lld:pubmed |
pubmed-article:7317006 | pubmed:volume | 196 | lld:pubmed |
pubmed-article:7317006 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7317006 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7317006 | pubmed:pagination | 657-62 | lld:pubmed |
pubmed-article:7317006 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:7317006 | pubmed:meshHeading | pubmed-meshheading:7317006-... | lld:pubmed |
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pubmed-article:7317006 | pubmed:meshHeading | pubmed-meshheading:7317006-... | lld:pubmed |
pubmed-article:7317006 | pubmed:year | 1981 | lld:pubmed |
pubmed-article:7317006 | pubmed:articleTitle | Compartmental distribution of beta-hexosaminidase isoenzymes in I-cell fibroblasts. | lld:pubmed |
pubmed-article:7317006 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7317006 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:7317006 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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