| pubmed-article:1991511 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1991511 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:1991511 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:1991511 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:1991511 | lifeskim:mentions | umls-concept:C0026140 | lld:lifeskim |
| pubmed-article:1991511 | lifeskim:mentions | umls-concept:C0008429 | lld:lifeskim |
| pubmed-article:1991511 | lifeskim:mentions | umls-concept:C0023764 | lld:lifeskim |
| pubmed-article:1991511 | lifeskim:mentions | umls-concept:C0024361 | lld:lifeskim |
| pubmed-article:1991511 | lifeskim:mentions | umls-concept:C0205681 | lld:lifeskim |
| pubmed-article:1991511 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:1991511 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:1991511 | lifeskim:mentions | umls-concept:C1710052 | lld:lifeskim |
| pubmed-article:1991511 | lifeskim:mentions | umls-concept:C2697616 | lld:lifeskim |
| pubmed-article:1991511 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1991511 | pubmed:dateCreated | 1991-3-13 | lld:pubmed |
| pubmed-article:1991511 | pubmed:abstractText | To determine the active site residue, human milk bile-salt stimulated lipase (BSSL) was labelled with [3H]diisopropyl fluorophosphate (DFP). Partial sequence analysis of cyanogen bromide fragments (a total of 146 residues from 6 peptides) revealed 84% sequence identity with a putative rat lysophospholipase. Sequence analysis of a [3H]DFP-labelled peptide indicated that the active site serine was contained in the sequence Gly-Glu-Ser-Ala-Gly. In addition to similarity with rat lysophospholipase, this sequence showed homology with regions of human butyrylcholinesterase and electric ray acetylcholinesterase (68% identity). It is concluded that these proteins are members of a new supergene family. | lld:pubmed |
| pubmed-article:1991511 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1991511 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1991511 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1991511 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1991511 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1991511 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1991511 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1991511 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1991511 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1991511 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1991511 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1991511 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:1991511 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:1991511 | pubmed:author | pubmed-author:ChristieD LDL | lld:pubmed |
| pubmed-article:1991511 | pubmed:author | pubmed-author:O'ConnorC JCJ | lld:pubmed |
| pubmed-article:1991511 | pubmed:author | pubmed-author:CleverlyD RDR | lld:pubmed |
| pubmed-article:1991511 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1991511 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:1991511 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:1991511 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1991511 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1991511 | pubmed:pagination | 190-4 | lld:pubmed |
| pubmed-article:1991511 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1991511 | pubmed:meshHeading | pubmed-meshheading:1991511-... | lld:pubmed |
| pubmed-article:1991511 | pubmed:meshHeading | pubmed-meshheading:1991511-... | lld:pubmed |
| pubmed-article:1991511 | pubmed:meshHeading | pubmed-meshheading:1991511-... | lld:pubmed |
| pubmed-article:1991511 | pubmed:meshHeading | pubmed-meshheading:1991511-... | lld:pubmed |
| pubmed-article:1991511 | pubmed:meshHeading | pubmed-meshheading:1991511-... | lld:pubmed |
| pubmed-article:1991511 | pubmed:meshHeading | pubmed-meshheading:1991511-... | lld:pubmed |
| pubmed-article:1991511 | pubmed:meshHeading | pubmed-meshheading:1991511-... | lld:pubmed |
| pubmed-article:1991511 | pubmed:meshHeading | pubmed-meshheading:1991511-... | lld:pubmed |
| pubmed-article:1991511 | pubmed:meshHeading | pubmed-meshheading:1991511-... | lld:pubmed |
| pubmed-article:1991511 | pubmed:meshHeading | pubmed-meshheading:1991511-... | lld:pubmed |
| pubmed-article:1991511 | pubmed:meshHeading | pubmed-meshheading:1991511-... | lld:pubmed |
| pubmed-article:1991511 | pubmed:meshHeading | pubmed-meshheading:1991511-... | lld:pubmed |
| pubmed-article:1991511 | pubmed:meshHeading | pubmed-meshheading:1991511-... | lld:pubmed |
| pubmed-article:1991511 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1991511 | pubmed:articleTitle | Human milk bile-salt stimulated lipase. Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases. | lld:pubmed |
| pubmed-article:1991511 | pubmed:affiliation | Department of Biochemistry, University of Auckland, New Zealand. | lld:pubmed |
| pubmed-article:1991511 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1991511 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:1991511 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:1056 | entrezgene:pubmed | pubmed-article:1991511 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1991511 | lld:pubmed |
