The spider Oligoctenus ornatus (Ctenidae) is very common in Brazil, occurring in regions of the Atlantic Forest, from Rio Grande Do Sul to the south of Bahia. Until recently, most of the studies on the venoms of the Ctenidae have been limited to the genus Phoneutria which are responsible for the majority of accidents of araneism in Brazil. These venoms contain a variety of bioactive molecules, peptides, neurotoxins that act in neuronal cells and enzymes. In spite of O. ornatus and Phoneutria belonging to the same family, so far there are no reports of the characterization of the venom of this spider. In this study we investigated the enzymatic profile in the venom of the spider O. ornatus (Oct). Initially, the crude venoms of Oct, males and females, were separately submitted to electrophoresis in polyacrylamide gels (SDS-PAGE, 15.0%). Various protein bands of high, average and low molecular masses were observed in these venoms. Quantitative differences between male and female venoms  were also noticed. Venom from Oct females appears to contain bands with higher concentrations of proteins than the venom of Oct males. Zymogram experiments using different substrates (Hyaluronic acid, glycol chitin and gelatin) showed the presence of hyaluronidase, chitinase and proteolytic enzymes in this venom. A protein band at approximately 37,0 kDa was noticed in 12.5% SDS-hyaluronic acid-PAGE gels, both in venoms from Oct males and females. Various bands of different molecular masses were found when the venoms were run in 10.0% SDS-PAGE gels which had glycol chitin incorporated into them, suggesting the presence of many chitinases enzymes in this venom. Colorless bands in an otherwise blue gel (SDS-PAGE- gelatin, 12.0%) showed the presence of gelatinolytic enzymes in Oct venom. The bands seemed stronger in the venom of the males than in the females. In addition, the alpha chain of fibrinogen was degraded when it was incubated with the venoms (male and female) during one hour at 37^oC, confirming the proteolytic activity. These enzymes from Oct are currenthy being purified.   Supported by: CNPq, FAPEMIG