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Fibrin(ogen)olytic and antiplatelet activities of a subtilisin-like protease from Solanum tuberosum (StSBTc-3)
(Elsevier France-editions Scientifiques Medicales Elsevier, 2016-06)
Plant serine proteases have been widely used in food science and technology as well as in medicine. In this sense, several plant serine proteases have been proposed as potential anti-coagulants and anti-platelet agents. ...
Purification from Bothrops lanceolatus (fer de lance) venom of a fibrino(geno)lytic enzyme with esterolytic activity
(Pergamon-elsevier Science LtdOxfordInglaterra, 1998)
Extração, caracterização e atividades biológicas de proteínas da espécie cnidoscolus urens (L.) Arthur
(Universidade Federal do Rio Grande do NorteBRUFRNPrograma de Pós-Graduação em Ciências FarmacêuticasBioanálises e Medicamentos, 2014)
Neutralization of pharmacological and toxic activities of Bothrops snake venoms by Schizolobium parahyba (Fabaceae) aqueous extract and its fractions
(WILEY-BLACKWELL, 2008)
The aqueous extract prepared from Schizolobium parahyba (Sp) leaves, a native plant from Atlantic Forest (Brazil), was tested to analyse its ability to inhibit some biological and enzymatic activities induced by Bothrops ...
Purificação e caracterização de uma nova metaloprotease da serpente Bothrops moojeni Hoge, 1966(Squamata: Viperidae) com ação na agregação plaquetária
(Universidade Federal de Minas GeraisUFMG, 2011-07-08)
Snake venoms contain a complex mixture of many different biologically active proteins and peptides. The present study aimed to evaluate the proteolytic and biological activities, as well as inhibitory effects on platelet ...
Isolation and structural characterization of a new fibrin(ogen)olytic metalloproteinase from Bothrops moojeni snake venom
(PERGAMON-ELSEVIER SCIENCE LTD, 2008)
A proteinase, named BmooMP alpha-I, from the venom of Bothrops moojeni, was purified by DEAE-Sephacel, Sephadex G-75 and heparin-agarose column chromatography. The enzyme was purified to homogeneity as judged by its migration ...
Insularinase A, a prothrombin activator from Bothrops insularis venom, is a metalloprotease derived from a gene encoding protease and disintegrin domains
(Walter de Gruyter Gmbh, 2005-06-01)
The first low-molecular-mass metalloprotease presenting prothrombin activating activity was purified from Bothrops insularis venom and named insularinase A. It is a single-chain protease with a molecular mass of 22 639 Da. ...
Caracterização estrutural e funcional de metaloproteases isoladas de peçonhas botrópicas
(Universidade Federal de UberlândiaBRPrograma de Pós-graduação em Genética e BioquímicaCiências BiológicasUFU, 2016)
Isolation and characterization of moojenin, an acid-active, anticoagulant metalloproteinase from Bothrops moojeni venom
(PERGAMON-ELSEVIER SCIENCE LTDOXFORD, 2012)
A fibrinogenolytic metalloproteinase from Bothrops moojeni venom, named moojenin, was purified by a combination of ion-exchange chromatography on DEAE-Sephacel and gel filtration on Sephacryl S-300. SDS-PAGE analysis ...