3093382

Source:http://linkedlifedata.com/resource/pubmed/id/3093382

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0004799, umls-concept:C0022984, umls-concept:C0208103, umls-concept:C0243125, umls-concept:C0333668, umls-concept:C0699900, umls-concept:C1563389, umls-concept:C1749467
pubmed:issue	1
pubmed:dateCreated	1986-11-7
pubmed:abstractText	Purified Pseudomonas aeruginosa elastase and alkaline protease rapidly cleaved soluble laminin, with each enzyme yielding different cleavage products. These cleavage fragments were separated from the intact laminin A and B polypeptide chains by sodium dodecyl sulfate-polyacrylamide gradient gel electrophoresis and detected by their characteristic Coomassie blue staining patterns. Pseudomonas elastase produced rapid and extensive degradation of both A and B chains, including the disulfide-rich regions. Apparently complete degradation to limit digests was obtained after 30 min with a substrate/enzyme ratio of 30:0.5. Under similar conditions, alkaline protease rapidly degraded the A chain while slowly degrading the B chain. In addition, immunoreactive laminin was released from authentic basement membranes after incubation with either enzyme as detected by an enzyme-linked immunoabsorption assay and by immunofluorescence. The results from these studies suggest a direct role for elastase and alkaline protease in both tissue invasion and hemorrhagic tissue necrosis in P. aeruginosa infections.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/1 RO1 AM 34972, http://linkedlifedata.com/resource/pubmed/grant/2 RO1 AM 03553, http://linkedlifedata.com/resource/pubmed/grant/AM 32073
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-106001, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-110690, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-110691, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-114518, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-14321366, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-14907713, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-3079727, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-3160113, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-3881623, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-3889015, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-3917980, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-4014440, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-4104239, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-415981, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-4199986, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-4210424, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-4370620, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-4954700, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-4959349, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-5004124, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-6210731, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-6228259, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-6401692, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-6405475, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-6427361, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-6439405, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-6439729, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-6791405, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-697880, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-7040076, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-7086353, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-7460011, http://linkedlifedata.com/resource/pubmed/commentcorrection/3093382-819684
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0246127
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Laminin, http://linkedlifedata.com/resource/pubmed/chemical/Pancreatic Elastase, http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/microbial serine proteinases
pubmed:status	MEDLINE
pubmed:month	Oct
pubmed:issn	0019-9567
pubmed:author	pubmed-author:AbrahamsonD RDR, pubmed-author:HeckL WLW, pubmed-author:MoriharaKK
pubmed:issnType	Print
pubmed:volume	54
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	149-53
pubmed:dateRevised	2009-11-18
pubmed:meshHeading	pubmed-meshheading:3093382-Animals, pubmed-meshheading:3093382-Basement Membrane, pubmed-meshheading:3093382-Endopeptidases, pubmed-meshheading:3093382-Extracellular Matrix, pubmed-meshheading:3093382-Fluorescent Antibody Technique, pubmed-meshheading:3093382-Laminin, pubmed-meshheading:3093382-Mice, pubmed-meshheading:3093382-Pancreatic Elastase, pubmed-meshheading:3093382-Pseudomonas aeruginosa, pubmed-meshheading:3093382-Serine Endopeptidases, pubmed-meshheading:3093382-Solubility
pubmed:year	1986
pubmed:articleTitle	Degradation of soluble laminin and depletion of tissue-associated basement membrane laminin by Pseudomonas aeruginosa elastase and alkaline protease.
pubmed:publicationType	Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.