| Bhalternin: Functional and structural characterization of a new thrombin-like enzyme from Bothrops alternatus snake venom. | |
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MedLine Citation:
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PMID: 20184912 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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A serine protease from Bothrops alternatus snake venom was isolated using DEAE-Sephacel, Sephadex G-75 and Benzamidine-Sepharose column chromatography. The purified enzyme, named Bhalternin, ran as a single protein band on analytical polyacrylamide gel electrophoresis (SDS-PAGE) and showed molecular weights of 31,500 and 27,000 under reducing and non-reducing conditions, respectively. Its complete cDNA was obtained by RT-PCR and the 708bp codified for a mature protein of 236 amino acid residues. The multiple alignment of its deduced amino acid sequence showed a structural similarly with other serine proteases from snake venoms. Bhalternin was proteolytically active against bovine fibrinogen and albumin as substrates. When Bhalternin and bovine fibrinogen were incubated at 37 degrees C, at a ratio of 1:100 (w/w), the enzyme cleaved preferentially the Aalpha-chain, apparently not degrading the Bbeta and gamma-chains. Stability tests showed that the intervals of optimum temperature and pH for the fibrinogenolytic activity were 30-40 degrees C and 7.0-8.0, respectively. Also, the inhibitory effects of benzamidine on the fibrinogenolytic activity of Bhalternin indicate that it is a serine protease. This enzyme caused morphological alterations in heart, liver, lung and muscle of mice and it was found to cause blood clotting in vitro and defibrinogenation when intraperitoneally administered to mice, suggesting it to be a thrombin-like enzyme. Therefore, Bhaltenin may be of interest as a therapeutic agent in the treatment and prevention of thrombotic disorders. |
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Authors:
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Júnia de O Costa; Kelly C Fonseca; Carla C Neves Mamede; Marcelo E Beletti; Norival A Santos-Filho; Andreimar M Soares; Eliane C Arantes; Silvia N S Hirayama; Heloísa S Selistre-de-Araújo; Fernando Fonseca; Flávio Henrique-Silva; Nilson Penha-Silva; Fábio de Oliveira |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-02-23 |
Journal Detail:
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Title: Toxicon : official journal of the International Society on Toxinology Volume: 55 ISSN: 1879-3150 ISO Abbreviation: Toxicon Publication Date: 2010 Jun |
Date Detail:
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Created Date: 2010-04-19 Completed Date: 2010-07-19 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 1307333 Medline TA: Toxicon Country: England |
Other Details:
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Languages: eng Pagination: 1365-77 Citation Subset: IM |
Copyright Information:
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2010 Elsevier Ltd. All rights reserved. |
Affiliation:
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Instituto de Genética e Bioquímica, Universidade Federal de Uberlândia, 38400-902 Uberlândia-MG, Brazil. juniacosta@iftriangulo.edu.br |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Albumins
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chemistry Amino Acid Sequence Animals Blood Coagulation / drug effects Bothrops* Caseins / chemistry Crotalid Venoms / enzymology*, pharmacology DNA, Complementary / biosynthesis, genetics Electrophoresis, Polyacrylamide Gel Exocrine Glands / chemistry Fibrinogen / chemistry Fibrinolytic Agents / pharmacology Gene Library Male Mice Molecular Sequence Data Molecular Weight Muscle, Skeletal / pathology Necrosis / chemically induced, pathology Peptide Hydrolases / chemistry Proteins / chemistry Serine Proteases / pharmacology Thrombin / chemistry* Viper Venoms / enzymology*, pharmacology |
| Chemical | |
Reg. No./Substance:
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0/Albumins; 0/Caseins; 0/Crotalid Venoms; 0/DNA, Complementary; 0/Fibrinolytic Agents; 0/Proteins; 0/Viper Venoms; 0/azocasein; 9001-32-5/Fibrinogen; EC 3.4.-/Peptide Hydrolases; EC 3.4.-/Serine Proteases; EC 3.4.-/bhalternin protein, Bothrops alternatus; EC 3.4.21.5/Thrombin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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