Batroxase, a new metalloproteinase from B. atrox snake venom with strong fibrinolytic activity

Toxicon

Volumn 60, Issue 1, 2012, Pages 70-82

  Cintra, A C O ^a   De Toni, L G B ^a   Sartim, M A ^a   Franco, J J ^a   Caetano, R C ^a   Murakami, M T ^b   Sampaio, S V ^a  

^a UNIVERSITY OF SÃO PAULO   (Brazil)

^b BRAZILIAN CENTER FOR RESEARCH IN ENERGY AND MATERIALS CNPEM   (Brazil)

Author keywords

Bothrops atrox venom; Fibrinolytic and thrombolytic activity; Snake venom metalloproteinase; Substrate specificity

Indexed keywords

BATROXASE; MATRIX METALLOPROTEINASE; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; BINDING SITE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME GLYCOSYLATION; ENZYME PURIFICATION; ENZYME STRUCTURE; FIBRINOLYSIS; MALE; MOLECULAR WEIGHT; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN MOTIF; SEQUENCE ANALYSIS; THROMBOCYTE AGGREGATION; TOXIN ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BOTHROPS; CROTALID VENOMS; FIBRINOLYSIS; ISOELECTRIC POINT; MASS SPECTROMETRY; METALLOPROTEASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; SEQUENCE HOMOLOGY, AMINO ACID;

BOTHROPS ATROX; BOTHROPS MOOJENI;

EID: 84859901810     PISSN: 00410101     EISSN: 18793150     Source Type: Journal    
DOI: 10.1016/j.toxicon.2012.03.018     Document Type: Article

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