Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2011-3-22
pubmed:abstractText
A new protease named NJP with fibrinolytic activity was isolated from Neanthes japonica (Izuka), by a combination of ammonium sulfate fractionation, hydrophobic chromatography, ion-exchange chromatography and gel filtration. The molecular mass of NJP was approximately 28.6-33.5kDa as estimated by MALDI-TOF mass spectrometry and SDS-PAGE, which revealed a monomeric form of the protease. The isoelectric point of NJP determined by 2-DE was 9.2. NJP was stable in the range of pH 7.0-11.0 with a maximum enzymatic activity at 40°C and pH 9.0. The hydrolyzing activity of NJP on fibrinogen started from the A?-chain, followed by the B?-chain, and the ?-chain at last. NJP had also a higher specificity for the chromogenic substrate S-2238 for thrombin. NJP activity was completely inhibited by PMSF. Analysis of partial amino acid sequences showed that NJP had very low homology with other known fibrinolytic enzymes. These results indicate that NJP is a novel alkaline thrombin-like serine protease. Thus NJP may have potential applications in the prevention and treatment of thrombosis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1879-1107
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
159
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18-25
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
A novel alkaline serine protease with fibrinolytic activity from the polychaete, Neanthes japonica.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Norman Bethune College of Medicine, Jilin University, 126 Xinmin Street, Changchun, Jilin, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't