Linked Life Data

9027985

Source:http://linkedlifedata.com/resource/pubmed/id/9027985

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11-12
pubmed:dateCreated
1997-5-8
pubmed:databankReference
pubmed:abstractText
Atroxase, isolated from the venom of Crotalus atrox (western diamondback rattlesnake), is a non-hemorrhagic protease which has fibrinolytic activity in vitro and in vivo. Fibrin solubilization occurs primarily from the hydrolysis of alpha-polymer and unpolymerized alpha- and beta-chains. The enzyme also cleaves the A alpha-chain of fibrinogen first, followed by the B beta-chain, and shows no effect on the gamma-chain. Although crude venom induces platelet aggregation, atroxase demonstrated no ability to induce or inhibit aggregation. Intravenous administration of atroxase at a dosage of 6.0 mg/kg resulted in thrombolysis within 1 hr followed by recanalization. The primary structure of atroxase was deduced from the cDNA encoding the atroxase protein. The venom glands of C. atrox were used to prepare a cDNA library. Degenerate oligonucleotides were synthesized based on the partial amino acid sequence of atroxase and were used as primers in the polymerase chain reaction to amplify overlapping cDNA fragments from the C. atrox cDNA library. The resulting cDNA fragments were subcloned, sequenced, and translated. The final nucleotide sequence shows high homology to previously described primary structures of non-hemorrhagic fibrinolytic proteases isolated from snake venom. The base sequence of cDNA obtained from colony hybridization also showed comparable results to the cDNA fragment amplified by PCR.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0041-0101
pubmed:author
pubmed:issnType
Print
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1295-300
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:articleTitle
Biochemical characterization of atroxase and nucleotide sequence encoding the fibrinolytic enzyme.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins 80523-1870, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't