| pubmed-article:411677 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:411677 | lifeskim:mentions | umls-concept:C0439660 | lld:lifeskim |
| pubmed-article:411677 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:411677 | lifeskim:mentions | umls-concept:C0178523 | lld:lifeskim |
| pubmed-article:411677 | lifeskim:mentions | umls-concept:C1283620 | lld:lifeskim |
| pubmed-article:411677 | lifeskim:mentions | umls-concept:C0205161 | lld:lifeskim |
| pubmed-article:411677 | lifeskim:mentions | umls-concept:C1317658 | lld:lifeskim |
| pubmed-article:411677 | lifeskim:mentions | umls-concept:C0150312 | lld:lifeskim |
| pubmed-article:411677 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:411677 | pubmed:dateCreated | 1978-1-27 | lld:pubmed |
| pubmed-article:411677 | pubmed:abstractText | In a child with hereditary sucrase-isomaltase deficiency immunoreactive enzyme was present in the intact duodenal mucosa. Polyacrylamide gel electrophoresis carried out with membrane fragments of an intestinal biopsy showed an abnormal protein band without enzyme activity. The mucosa had a relatively high residual isomaltase activity which was recovered from the gel in a position suggesting higher than normal molecular weight. The results indicated that in this patient the primary structural defect was in the sucrase moiety which was enzymatically inactive. The isomaltase subunits may have aggregated into a large molecular weight complex because of unavailability of their partners. The observation also provided evidence for separate biosynthesis of the two moieties of the sucrase-isomaltase complex. | lld:pubmed |
| pubmed-article:411677 | pubmed:language | eng | lld:pubmed |
| pubmed-article:411677 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:411677 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:411677 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:411677 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:411677 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:411677 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:411677 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:411677 | pubmed:issn | 0014-2972 | lld:pubmed |
| pubmed-article:411677 | pubmed:author | pubmed-author:GitzelmannRR | lld:pubmed |
| pubmed-article:411677 | pubmed:author | pubmed-author:HadornBB | lld:pubmed |
| pubmed-article:411677 | pubmed:author | pubmed-author:GazeHH | lld:pubmed |
| pubmed-article:411677 | pubmed:author | pubmed-author:EWENKK | lld:pubmed |
| pubmed-article:411677 | pubmed:author | pubmed-author:HauriH PHP | lld:pubmed |
| pubmed-article:411677 | pubmed:author | pubmed-author:FreiburghausA... | lld:pubmed |
| pubmed-article:411677 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:411677 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:411677 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:411677 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:411677 | pubmed:pagination | 455-9 | lld:pubmed |
| pubmed-article:411677 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
| pubmed-article:411677 | pubmed:meshHeading | pubmed-meshheading:411677-H... | lld:pubmed |
| pubmed-article:411677 | pubmed:meshHeading | pubmed-meshheading:411677-C... | lld:pubmed |
| pubmed-article:411677 | pubmed:meshHeading | pubmed-meshheading:411677-M... | lld:pubmed |
| pubmed-article:411677 | pubmed:meshHeading | pubmed-meshheading:411677-F... | lld:pubmed |
| pubmed-article:411677 | pubmed:meshHeading | pubmed-meshheading:411677-M... | lld:pubmed |
| pubmed-article:411677 | pubmed:meshHeading | pubmed-meshheading:411677-C... | lld:pubmed |
| pubmed-article:411677 | pubmed:meshHeading | pubmed-meshheading:411677-F... | lld:pubmed |
| pubmed-article:411677 | pubmed:meshHeading | pubmed-meshheading:411677-M... | lld:pubmed |
| pubmed-article:411677 | pubmed:meshHeading | pubmed-meshheading:411677-E... | lld:pubmed |
| pubmed-article:411677 | pubmed:meshHeading | pubmed-meshheading:411677-M... | lld:pubmed |
| pubmed-article:411677 | pubmed:meshHeading | pubmed-meshheading:411677-S... | lld:pubmed |
| pubmed-article:411677 | pubmed:year | 1977 | lld:pubmed |
| pubmed-article:411677 | pubmed:articleTitle | The brush border membrane in hereditary sucrase-isomaltase deficiency: abnormal protein pattern and presence of immunoreactive enzyme. | lld:pubmed |
| pubmed-article:411677 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:411677 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:411677 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:411677 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:411677 | lld:pubmed |
