{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T08:16:58Z","timestamp":1790756218340,"version":"4.1.0"},"reference-count":48,"publisher":"Wiley","issue":"17","license":[{"start":{"date-parts":[[2001,8,10]],"date-time":"2001-08-10T00:00:00Z","timestamp":997401600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Rapid Comm Mass Spectrometry"],"published-print":{"date-parts":[[2001,9,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Scorpion venoms are very complex mixtures of molecules, most of which are peptides that display different kinds of biological activity. These venoms have been studied in the light of their pharmacological targets and their constituents are able to bind specifically to a variety of ionic channels located in prey tissues, resulting in neurotoxic effects. Toxins that modulate Na\n                    <jats:sup>+<\/jats:sup>\n                    , K\n                    <jats:sup>+<\/jats:sup>\n                    , Ca\n                    <jats:sup>++<\/jats:sup>\n                    and Cl\n                    <jats:sup>\u2212<\/jats:sup>\n                    currents have been described in scorpion venoms. Mass spectrometry was employed to analyze toxic fractions from the venom of the Brazilian scorpion\n                    <jats:italic>Tityus serrulatus<\/jats:italic>\n                    in order to shed light on the molecular composition of this venom and to facilitate the search for novel pharmacologically active compounds.\n                    <jats:italic>T. serrulatus<\/jats:italic>\n                    venom was first subjected to gel filtration to separate its constituents according to their molecular size. The resultant fractions II and III, which account for 90 and 10% respectively of the whole venom toxic effect, were further analyzed by matrix\u2010assisted laser desorption\/ionization time\u2010of\u2010flight mass spectrometry (MALDI\u2010TOFMS), on\u2010line liquid chromatography\/electrospray mass spectrometry (LC\/ESMS) and off\u2010line LC\/MALDI\u2010TOFMS in order to establish their mass fingerprints. The molecular masses in fraction II were predominantly between 6500 and 7500\u2005Da. This corresponds to long\u2010chain toxins that mainly act on voltage\u2010gated Na\n                    <jats:sup>+<\/jats:sup>\n                    channels. Fraction III is more complex and predominantly contained molecules with masses between 2500 and 5000\u2005Da. This corresponds to the short\u2010chain toxin family, most of which act on K\n                    <jats:sup>+<\/jats:sup>\n                    channels, and other unknown peptides. Finally, we were able to measure the molecular masses of 380 different compounds present in the two fractions investigated. To our knowledge, this is the largest number of components ever detected in the venom of a single animal species. Some of the toxins described previously from\n                    <jats:italic>T. serrulatus<\/jats:italic>\n                    venom could be detected by virtue of their molecular masses. The interpretation of this large set of data has provided us with useful proteomic information on the venom, and the implications of these findings are discussed. Copyright \u00a9 2001 John Wiley &amp; Sons, Ltd.\n                  <\/jats:p>","DOI":"10.1002\/rcm.415","type":"journal-article","created":{"date-parts":[[2002,8,25]],"date-time":"2002-08-25T15:56:46Z","timestamp":1030291006000},"page":"1562-1572","source":"Crossref","is-referenced-by-count":103,"title":["Moving pieces in a proteomic puzzle: mass fingerprinting of toxic fractions from the venom of\n                    <i>Tityus serrulatus<\/i>\n                    (Scorpiones, Buthidae)"],"prefix":"10.1002","volume":"15","author":[{"given":"Adriano M. 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