Partial Characterization Of Fibrinogenolytic Enzyme Purified From Bothrops moojeni Snake Venom.

¹Costa, J. de O.; ¹Izidoro, L. F. M.; ¹Hamaguchi, A.; ¹Homsi-Brandeburgo, M. I. and ²Oliveira, F.

1 Instituto de Genética e Bioquímica, 2 Departamento de Ciências Fisiológicas/Instituto de Ciências Biomédicas, Universidade Federal de Uberlândia, Minas Gerais, Brasil.

This work describes the purification of a -fibrinogenolytic enzyme from the venom of Bothropsmoojeni This enzyme, designed Moojenase, was purified. by DEAE- Sephacel and Sephadex G-75 chromatographies. Moojenase was shown to be homogeneous with molecular mass of about 24 kDa as demonstrated by SDS-PAGE. The enzyme is devoid of hemorrhagic, phospholipase A2 and plasma coagulant activities and shows a high proteolytic activity towards A-a and B-b chains of bovine fibrinogen. In addition, Moojenase caused blood incoagulability when administered i. p. in mice. The fibrinogen levels became very low after 1 hour of the injection of 5 mg of the enzyme. The normal  levels were only reestablished after 24 hours. The fibrinogenolytic activity of the enzyme was inhibited by PMSF, EDTA, EGTA, b-mercaptoetanol and presents maximum activity in a alkaline pH range. This enzyme can be promising as an alternative for the therapeutical use as antithrombotic agent or in combination with other trombolytic agents.

Support: CAPES, CNPq, FAPEMIG and UFU.

Correspondence to: lfmizidoro@zipmail.com.br