Linked Life Data

19129947

Source:http://linkedlifedata.com/resource/pubmed/id/19129947

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2009-1-8
pubmed:abstractText
Fibrinogen-activating enzymes, widely distributed in Crotalidae and Viperidae venoms, are single-chain glycosylated serine proteases that display high macromolecular selectivity and are often referred to as thrombin-like enzymes (TLEs). TLEs serve as structural models to extend our understanding of the structure-function relationships of blood coagulation factors, have been clinically used for the treatment of thrombotic diseases, and are used as tools in clinical assays. The combination of gel filtration and ion-exchange chromatography proved to be successful in obtaining milligram quantities of pure samples of TLEs from the venoms of Crotalus durissus terrificus (white venom) and Crotalus durissus collilineatus (yellow venom). Functional characterization indicates that both enzymes preferentially degrade the Bb chain of bovine fibrinogen and possess edema-inducing and coagulant activities. However, the TLE from C. d. collilineatus venom shows twofold higher coagulant activity with a minimum coagulant dose (MCD) of 0.6 microg/microl, whereas the enzyme isolated from C. d. terrificus indicated an MCD of 1.5 microg/microl. Molecular modeling of gyroxin and structural comparisons with other highly conserved snake venom serine proteases, underlines the key role played by the surface charge distribution and the double insertion in the 174-surface loop in macromolecular substrate recognition by TLEs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1745-7270
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21-9
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Functional and structural analysis of two fibrinogen-activating enzymes isolated from the venoms of Crotalus durissus terrificus and Crotalus durissus collilineatus.
pubmed:affiliation
Department of Physics, Center for Structural & Molecular Biology, IBILCE/UNESP, São José do Rio Preto, SP, Brazil
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't