| pubmed-article:3242555 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3242555 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:3242555 | lifeskim:mentions | umls-concept:C0038727 | lld:lifeskim |
| pubmed-article:3242555 | lifeskim:mentions | umls-concept:C1419116 | lld:lifeskim |
| pubmed-article:3242555 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:3242555 | lifeskim:mentions | umls-concept:C2003939 | lld:lifeskim |
| pubmed-article:3242555 | lifeskim:mentions | umls-concept:C1157953 | lld:lifeskim |
| pubmed-article:3242555 | lifeskim:mentions | umls-concept:C0205197 | lld:lifeskim |
| pubmed-article:3242555 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:3242555 | pubmed:dateCreated | 1989-6-8 | lld:pubmed |
| pubmed-article:3242555 | pubmed:abstractText | The naturally occurring A2 activator protein for enzymic sphingolipid degradation is characterized by complete amino-acid sequence and carbohydrate content. It consists of 79 amino-acid residues and has a molecular mass of 8.875 kDa. The polypeptide chain contains 2 mol of N-acetylglucosamine, bound to asparagine in position 21, as well as 2 mol of galactose and mannose per mol protein. The primary structure of the A2 activator protein is identical to that of the sulfatide activator protein (SAP-1). Possible differences in the carbohydrate content are discussed. | lld:pubmed |
| pubmed-article:3242555 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3242555 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3242555 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3242555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3242555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3242555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3242555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3242555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3242555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3242555 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3242555 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:3242555 | pubmed:issn | 0177-3593 | lld:pubmed |
| pubmed-article:3242555 | pubmed:author | pubmed-author:BraunitzerGG | lld:pubmed |
| pubmed-article:3242555 | pubmed:author | pubmed-author:ChristomanouH... | lld:pubmed |
| pubmed-article:3242555 | pubmed:author | pubmed-author:KleinschmidtT... | lld:pubmed |
| pubmed-article:3242555 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3242555 | pubmed:volume | 369 | lld:pubmed |
| pubmed-article:3242555 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3242555 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3242555 | pubmed:pagination | 1361-5 | lld:pubmed |
| pubmed-article:3242555 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:3242555 | pubmed:meshHeading | pubmed-meshheading:3242555-... | lld:pubmed |
| pubmed-article:3242555 | pubmed:meshHeading | pubmed-meshheading:3242555-... | lld:pubmed |
| pubmed-article:3242555 | pubmed:meshHeading | pubmed-meshheading:3242555-... | lld:pubmed |
| pubmed-article:3242555 | pubmed:meshHeading | pubmed-meshheading:3242555-... | lld:pubmed |
| pubmed-article:3242555 | pubmed:meshHeading | pubmed-meshheading:3242555-... | lld:pubmed |
| pubmed-article:3242555 | pubmed:meshHeading | pubmed-meshheading:3242555-... | lld:pubmed |
| pubmed-article:3242555 | pubmed:meshHeading | pubmed-meshheading:3242555-... | lld:pubmed |
| pubmed-article:3242555 | pubmed:meshHeading | pubmed-meshheading:3242555-... | lld:pubmed |
| pubmed-article:3242555 | pubmed:meshHeading | pubmed-meshheading:3242555-... | lld:pubmed |
| pubmed-article:3242555 | pubmed:meshHeading | pubmed-meshheading:3242555-... | lld:pubmed |
| pubmed-article:3242555 | pubmed:meshHeading | pubmed-meshheading:3242555-... | lld:pubmed |
| pubmed-article:3242555 | pubmed:meshHeading | pubmed-meshheading:3242555-... | lld:pubmed |
| pubmed-article:3242555 | pubmed:meshHeading | pubmed-meshheading:3242555-... | lld:pubmed |
| pubmed-article:3242555 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3242555 | pubmed:articleTitle | Complete amino-acid sequence of the naturally occurring A2 activator protein for enzymic sphingomyelin degradation: identity to the sulfatide activator protein (SAP-1). | lld:pubmed |
| pubmed-article:3242555 | pubmed:affiliation | Max-Planck-Institut für Biochemie, Martinsried bei München. | lld:pubmed |
| pubmed-article:3242555 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3242555 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:5660 | entrezgene:pubmed | pubmed-article:3242555 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3242555 | lld:pubmed |
