rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1996-12-5
|
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.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0014-5793
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
30
|
pubmed:volume |
394
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
179-82
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:8843159-Amino Acid Sequence,
pubmed-meshheading:8843159-Antibodies, Monoclonal,
pubmed-meshheading:8843159-Blotting, Western,
pubmed-meshheading:8843159-Endopeptidases,
pubmed-meshheading:8843159-Isoflurophate,
pubmed-meshheading:8843159-Kinetics,
pubmed-meshheading:8843159-Molecular Sequence Data,
pubmed-meshheading:8843159-Peptides,
pubmed-meshheading:8843159-Porins,
pubmed-meshheading:8843159-Pseudomonas aeruginosa,
pubmed-meshheading:8843159-Sequence Alignment,
pubmed-meshheading:8843159-Serine Endopeptidases
|
pubmed:year |
1996
|
pubmed:articleTitle |
Protein D2 porin of the Pseudomonas aeruginosa outer membrane bears the protease activity.
|
pubmed:affiliation |
Department of Molecular Life Science, Tokai University School of Medicine, Isehara, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|