| pubmed-article:8843159 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8843159 | lifeskim:mentions | umls-concept:C0033809 | lld:lifeskim |
| pubmed-article:8843159 | lifeskim:mentions | umls-concept:C0004897 | lld:lifeskim |
| pubmed-article:8843159 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8843159 | lifeskim:mentions | umls-concept:C1167331 | lld:lifeskim |
| pubmed-article:8843159 | lifeskim:mentions | umls-concept:C0071728 | lld:lifeskim |
| pubmed-article:8843159 | lifeskim:mentions | umls-concept:C2263455 | lld:lifeskim |
| pubmed-article:8843159 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8843159 | pubmed:dateCreated | 1996-12-5 | lld:pubmed |
| pubmed-article:8843159 | pubmed:abstractText | We report here our discovery that protein D2 of the outer membrane of Pseudomonas aeruginosa is a novel porin bearing protease activity. Homogeneously purified protein D2 hydrolyzed several synthetic peptides according to the Michaelis-Menten kinetics. A specific serine protease inhibitor, diisopropyl fluorophosphate (DFP), inactivated the protease activity and [3H]DFP covalently labeled protein D2. We tested the effect of two monoclonal antibodies raised against protein D2 on the protease activity. One antibody lowered the protease activity to about 20%, while the other enhanced it to about 300% of that without antibody. In addition, the fractions derived from the outer membrane of the protein D2-deficient mutants showed negligible protease activity, whereas similarly fractionated outer membrane proteins of the protein D2-positive parent strain showed strong protease activity. | lld:pubmed |
| pubmed-article:8843159 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8843159 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8843159 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8843159 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8843159 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8843159 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8843159 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8843159 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8843159 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8843159 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8843159 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8843159 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8843159 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:8843159 | pubmed:author | pubmed-author:NishinoTT | lld:pubmed |
| pubmed-article:8843159 | pubmed:author | pubmed-author:NakaeTT | lld:pubmed |
| pubmed-article:8843159 | pubmed:author | pubmed-author:YoshiharaEE | lld:pubmed |
| pubmed-article:8843159 | pubmed:author | pubmed-author:GotohNN | lld:pubmed |
| pubmed-article:8843159 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8843159 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:8843159 | pubmed:volume | 394 | lld:pubmed |
| pubmed-article:8843159 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8843159 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8843159 | pubmed:pagination | 179-82 | lld:pubmed |
| pubmed-article:8843159 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8843159 | pubmed:meshHeading | pubmed-meshheading:8843159-... | lld:pubmed |
| pubmed-article:8843159 | pubmed:meshHeading | pubmed-meshheading:8843159-... | lld:pubmed |
| pubmed-article:8843159 | pubmed:meshHeading | pubmed-meshheading:8843159-... | lld:pubmed |
| pubmed-article:8843159 | pubmed:meshHeading | pubmed-meshheading:8843159-... | lld:pubmed |
| pubmed-article:8843159 | pubmed:meshHeading | pubmed-meshheading:8843159-... | lld:pubmed |
| pubmed-article:8843159 | pubmed:meshHeading | pubmed-meshheading:8843159-... | lld:pubmed |
| pubmed-article:8843159 | pubmed:meshHeading | pubmed-meshheading:8843159-... | lld:pubmed |
| pubmed-article:8843159 | pubmed:meshHeading | pubmed-meshheading:8843159-... | lld:pubmed |
| pubmed-article:8843159 | pubmed:meshHeading | pubmed-meshheading:8843159-... | lld:pubmed |
| pubmed-article:8843159 | pubmed:meshHeading | pubmed-meshheading:8843159-... | lld:pubmed |
| pubmed-article:8843159 | pubmed:meshHeading | pubmed-meshheading:8843159-... | lld:pubmed |
| pubmed-article:8843159 | pubmed:meshHeading | pubmed-meshheading:8843159-... | lld:pubmed |
| pubmed-article:8843159 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8843159 | pubmed:articleTitle | Protein D2 porin of the Pseudomonas aeruginosa outer membrane bears the protease activity. | lld:pubmed |
| pubmed-article:8843159 | pubmed:affiliation | Department of Molecular Life Science, Tokai University School of Medicine, Isehara, Japan. | lld:pubmed |
| pubmed-article:8843159 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8843159 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8843159 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8843159 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8843159 | lld:pubmed |
