Snake venom metalloproteinases (SVMPs) represent a diverse group of multi-domain
proteins with several biological activities such as the ability to induce hemorrhage …

As more data are generated from proteome and transcriptome analyses of snake venoms,
we are gaining an appreciation of the complexity of the venoms and, to some degree, the …

The Handbook of Venoms and Toxins of Reptiles offers" one-stop shopping" to all biologists,
biochemists, toxicologists, physicians, clinicians, and epidemiologists, and informed …

The structures and functional activities of metalloproteinases from snake venoms have been
widely studied because of the importance of these molecules in envenomation. Batroxase …

Comparisons between venoms from snakes kept under captivity or collected at the natural
environment are of fundamental importance in order to obtain effective antivenoms to treat …

Ontogenetic changes in venom composition have been described in Bothrops snakes, but
only a few studies have attempted to identify the targeted paralogues or the molecular …

We report here the antiproteolytic and antihemorrhagic properties of triterpenoid saponin
inhibitors, named macrolobin-A and B, from Pentaclethra macroloba, against Bothrops …

Snake venom metalloproteinases (SVMPs) are abundant in the venoms of vipers and
rattlesnakes, playing important roles for the snake adaptation to different environments, and …

A proteinase, named BmooMPα-I, from the venom of Bothrops moojeni, was purified by
DEAE-Sephacel, Sephadex G-75 and heparin-agarose column chromatography. The …

A new l-amino acid oxidase (LAAO) from Bothrops jararacussu venom (BjussuLAAO-II) was
isolated by using a three-step chromatographic procedure based on molecular exclusion …