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Inhibition of proteases, myotoxins and phospholipases A2 from Bothrops venoms by the heteromeric protein complex of Didelphis albiventris opossum serum
Author(s) -
Soares A. M.,
Rodrigues V. M.,
Borges M. H.,
AndriãoEscarso S. H.,
Cunha O. A. B.,
HomsiBrandeburgo M. I.,
Giglio J. R.
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700204911
Subject(s) - bothrops , bothrops jararaca , opossum , venom , didelphis , myotoxin , snake venom , biology , chemistry , biochemistry , anatomy
The antibothropic complex (ABC) from opossum (species Didelphis albiventris) serum was purified by chromatography on DEAE‐Sephacel. It showed an acidic character and two polypeptide chains of ca. 45 kDa and 48 kDa, respectively. Lyophilized opossum serum or the ABC (1001μg), as well as ethylenediamine tetraacetate (0.25μmotes) were able to completely neutralise the hemorrhagic effect of 50μg of the desiccated venoms of Bothrops moojeni, Bothrops pirajai and Bothrops jararacussu. The myotoxic (100μg venom in mice) and edematogenic (90μg venom in rats) activities of Bothrops moojeni and Bothrops jararacussu venoms, as well as of the major myonecrotic protein (myotoxin‐I) isolated from Bothrops moojeni venom, were also totally inhibited by the ABC (200μg and 270μg, respectively). The lyophilized opossum serum (30μg) and the ABC (30μg) reduced to 50% the phospholipase A2 activity of Bothrops moojeni venom (10μg). The clotting activity of Bothrops alternatus and Bothrops moojeni (20μg) on bovine plasma was also significantly inhibited by the ABC (60μg).