Literature DB >> 12165326

N-terminal amino acid sequences and some characteristics of fibrinolytic/hemorrhagic metalloproteinases purified from Bothrops jararaca venom.

Masugi Maruyama1, Masahiko Sugiki, Keita Anai, Etsuo Yoshida.   

Abstract

We determined the N-terminal amino acid sequences of the fibrinolytic/hemorrhagic metalloproteinases (jararafibrases I, III and IV) purified from Bothrops jararaca venom. The N-terminal amino acid sequences of jararafibrase I and its degradation products were identical to those of jararhagin, another hemorrhagic metalloproteinase purified from the same snake venom. Together with enzymatic and immunological properties, we concluded that those two enzymes are identical. The N-terminal amino acid sequence of jararafibrase III was quite similar to C-type lectin isolated from Crotalus atrox, and the protein had a hemagglutinating activity on intact rat red blood cells.

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Year:  2002        PMID: 12165326     DOI: 10.1016/s0041-0101(02)00116-2

Source DB:  PubMed          Journal:  Toxicon        ISSN: 0041-0101            Impact factor:   3.033


  3 in total

1.  Purification and characterization of a new weak hemorrhagic metalloproteinase BmHF-1 from Bothrops marajoensis snake venom.

Authors:  Frank Denis Torres-Huaco; Luis Alberto Ponce-Soto; Daniel Martins-de-Souza; Sergio Marangoni
Journal:  Protein J       Date:  2010-08       Impact factor: 2.371

2.  Bmoo FIBMP-I: A New Fibrinogenolytic Metalloproteinase from Bothrops moojeni Snake Venom.

Authors:  F S Torres; B Rates; M T R Gomes; C E Salas; A M C Pimenta; F Oliveira; M M Santoro; M E de Lima
Journal:  ISRN Toxicol       Date:  2012-11-04

3.  Bothrops jararaca venom metalloproteinases are essential for coagulopathy and increase plasma tissue factor levels during envenomation.

Authors:  Karine M Yamashita; André F Alves; Katia C Barbaro; Marcelo L Santoro
Journal:  PLoS Negl Trop Dis       Date:  2014-05-15
  3 in total

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