Linked Life Data

2939587

Source:http://linkedlifedata.com/resource/pubmed/id/2939587

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1986-6-9
pubmed:abstractText
An anticoagulant enzyme, Cerastase F-4, from the venom of Cerastes cerastes was purified to homogeneity and was characterized (1). In the present report the mode of its fibrinogenolytic and fibrinolytic actions, and its effects on some other blood coagulation factors are described. Cerastes F-4 was shown to readily hydrolyze the alpha A chain of fibrinogen followed by the hydrolysis of the beta B chain. The gamma-chain was relatively resistant to hydrolysis. It also degrades the three chains of fibrin at different rates. The degradation products of the two substrates shown on SDS-polyacrylamide gel were quite different from those produced by plasmin, indicating different sites of cleavage by the enzyme. Using specific chromogenic substrates, Cerastase F-4 seems not to show thrombin-like, plasmin-like, kallikrein-like, antithrombin, or antiplasmin actions. Also, it does not activate prothrombin or plasminogen but degrades both of them slowly. It is concluded that the anticoagulation property of the purified enzyme, Cerastase F-4, is due to its destruction of fibrinogen.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0049-3848
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
791-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Mechanism of the anticoagulant, Cerastase F-4, isolated from Cerastes cerastes (Egyptian sand viper) venom.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't