| pubmed-article:6511787 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6511787 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:6511787 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
| pubmed-article:6511787 | lifeskim:mentions | umls-concept:C0014467 | lld:lifeskim |
| pubmed-article:6511787 | lifeskim:mentions | umls-concept:C0024361 | lld:lifeskim |
| pubmed-article:6511787 | lifeskim:mentions | umls-concept:C0055271 | lld:lifeskim |
| pubmed-article:6511787 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:6511787 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:6511787 | pubmed:dateCreated | 1985-1-25 | lld:pubmed |
| pubmed-article:6511787 | pubmed:abstractText | Lysophospholipase from human eosinophils is a protein previously considered based upon antigenic, enzymatic, and electrophoretic similarities to be the single component of Charcot-Leyden crystals, which are formed in vivo in association with eosinophilic diseases. The identity of eosinophil lysophospholipase and solubilized Charcot-Leyden crystal protein is now established by biochemical criteria, and a basis for the ease of aggregation and crystallization of the protein is identified in its prominent hydrophobicity. Chromatographically purified enzyme and Charcot-Leyden crystal protein formed in vitro functioned as lysophospholipases with identical Michaelis constants (Km approximately equal to 22 microM) for the substrate lysopalmitoylphosphatidylcholine and had blocked amino-terminal residues and almost identical amino acid compositions. The propensity of lysophospholipase to aggregate was not due to extensive intermolecular disulfide bonding because it contained a single cysteine residue as assessed by amino acid analyses and incorporated 0.986 mol of p-chloromercuribenzoic acid/mol of native enzyme or 0.958 mol of iodoacetic acid/mol of reduced and denatured enzyme. By equilibrium dialysis, lysophospholipase bound 3.820 g of detergent/g of protein in 1% sodium dodecyl sulfate and 0.506 g of detergent/g of protein in 10 mM sodium deoxycholate. In addition, monomeric protein demonstrated enhanced binding of detergent as evidenced by its aberrantly rapid electrophoretic mobility in 1%, but not 0.1%, sodium dodecyl sulfate. The hydrophobic nature of this protein, which accounts for 10% of the protein of the eosinophil, may contribute to its unique propensity for crystallization in vivo. | lld:pubmed |
| pubmed-article:6511787 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6511787 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6511787 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6511787 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6511787 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6511787 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6511787 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6511787 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:6511787 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6511787 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:6511787 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:6511787 | pubmed:author | pubmed-author:AustenK FKF | lld:pubmed |
| pubmed-article:6511787 | pubmed:author | pubmed-author:WellerP FPF | lld:pubmed |
| pubmed-article:6511787 | pubmed:author | pubmed-author:BachD SDS | lld:pubmed |
| pubmed-article:6511787 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6511787 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:6511787 | pubmed:volume | 259 | lld:pubmed |
| pubmed-article:6511787 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6511787 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6511787 | pubmed:pagination | 15100-5 | lld:pubmed |
| pubmed-article:6511787 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:6511787 | pubmed:meshHeading | pubmed-meshheading:6511787-... | lld:pubmed |
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| pubmed-article:6511787 | pubmed:meshHeading | pubmed-meshheading:6511787-... | lld:pubmed |
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| pubmed-article:6511787 | pubmed:meshHeading | pubmed-meshheading:6511787-... | lld:pubmed |
| pubmed-article:6511787 | pubmed:meshHeading | pubmed-meshheading:6511787-... | lld:pubmed |
| pubmed-article:6511787 | pubmed:meshHeading | pubmed-meshheading:6511787-... | lld:pubmed |
| pubmed-article:6511787 | pubmed:meshHeading | pubmed-meshheading:6511787-... | lld:pubmed |
| pubmed-article:6511787 | pubmed:meshHeading | pubmed-meshheading:6511787-... | lld:pubmed |
| pubmed-article:6511787 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6511787 | pubmed:articleTitle | Biochemical characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase). | lld:pubmed |
| pubmed-article:6511787 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6511787 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6511787 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:1178 | entrezgene:pubmed | pubmed-article:6511787 | lld:entrezgene |
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