pubmed-article:2451538 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2451538 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
pubmed-article:2451538 | lifeskim:mentions | umls-concept:C0033809 | lld:lifeskim |
pubmed-article:2451538 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:2451538 | lifeskim:mentions | umls-concept:C0071728 | lld:lifeskim |
pubmed-article:2451538 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
pubmed-article:2451538 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:2451538 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:2451538 | pubmed:dateCreated | 1988-5-18 | lld:pubmed |
pubmed-article:2451538 | pubmed:abstractText | A large-scale purification scheme was developed for lipopolysaccharide-free protein P, the phosphate-starvation-inducible outer-membrane porin from Pseudomonas aeruginosa. This highly purified protein P was used to successfully form hexagonal crystals in the presence of n-octyl-beta-glucopyranoside. Amino-acid analysis indicated that protein P had a similar composition to other bacterial outer membrane proteins, containing a high percentage (50%) of hydrophilic residues. The amino-terminal sequence of this protein, although not homologous to either outer membrane protein, PhoE or OmpF, of Escherichia coli, was found to have an analogous protein-folding pattern. Protein P in the native trimer form was capable of maintaining a stable functional trimer after proteinase cleavage. This suggested the existence of a strongly associated tertiary and quaternary structure. Circular dichroism studies confirmed these results in that a large proportion of the protein structure was determined to be beta-sheet and resistant to acid pH and heating in 0.1% sodium dodecyl sulphate. | lld:pubmed |
pubmed-article:2451538 | pubmed:language | eng | lld:pubmed |
pubmed-article:2451538 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2451538 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2451538 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:2451538 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2451538 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2451538 | pubmed:month | Apr | lld:pubmed |
pubmed-article:2451538 | pubmed:issn | 0006-3002 | lld:pubmed |
pubmed-article:2451538 | pubmed:author | pubmed-author:KayC MCM | lld:pubmed |
pubmed-article:2451538 | pubmed:author | pubmed-author:McCubbinW DWD | lld:pubmed |
pubmed-article:2451538 | pubmed:author | pubmed-author:BrayerG DGD | lld:pubmed |
pubmed-article:2451538 | pubmed:author | pubmed-author:HancockR ERE | lld:pubmed |
pubmed-article:2451538 | pubmed:author | pubmed-author:MartinN LNL | lld:pubmed |
pubmed-article:2451538 | pubmed:author | pubmed-author:WorobecE AEA | lld:pubmed |
pubmed-article:2451538 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2451538 | pubmed:day | 7 | lld:pubmed |
pubmed-article:2451538 | pubmed:volume | 939 | lld:pubmed |
pubmed-article:2451538 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2451538 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2451538 | pubmed:pagination | 366-74 | lld:pubmed |
pubmed-article:2451538 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:2451538 | pubmed:year | 1988 | lld:pubmed |
pubmed-article:2451538 | pubmed:articleTitle | Large-scale purification and biochemical characterization of crystallization-grade porin protein P from Pseudomonas aeruginosa. | lld:pubmed |
pubmed-article:2451538 | pubmed:affiliation | Department of Microbiology, University of British Columbia, Vancouver, Canada. | lld:pubmed |
pubmed-article:2451538 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2451538 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:2451538 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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