Linked Life Data

18805500

Source:http://linkedlifedata.com/resource/pubmed/id/18805500

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2008-11-17
pubmed:abstractText
Fibrinogen is an essential protein involved in several steps of hemostasis, being associated with the final steps of the blood coagulation mechanism. Herein, we describe the purification and characterization of a reptile fibrinogen, obtained from Bothrops jararaca plasma. Native B. jararaca fibrinogen showed a molecular mass of 372 kDa, and the reduced and alkylated fibrinogen molecule showed three chains of 71, 60 and 55 kDa, which are similar to the molecular masses of human and bovine Aalpha, Bbeta and gamma fibrinogen chains. Remarkably, B. jararaca fibrinogen was clotted by bovine thrombin, but B. jararaca, Crotalus durissus terrificus and Lachesis muta rhombeata venoms could not induce its clotting or hydrolysis. Thus, despite the similarities between B. jararaca and mammalian fibrinogens, the former shows distinctive features, which protect B. jararaca snakes from accidental envenomation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1879-1107
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
151
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
428-32
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Bothrops jararaca fibrinogen and its resistance to hydrolysis evoked by snake venoms.
pubmed:affiliation
Laboratory of Pathophysiology, Butantan Institute, São Paulo, Brazil.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't