{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T08:45:02Z","timestamp":1791189902490,"version":"4.1.0"},"reference-count":36,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2005,5,23]],"date-time":"2005-05-23T00:00:00Z","timestamp":1116806400000},"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":[[2005,6,30]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Characterization of the peptide content in snake venoms can be an important tool for the investigation of new pharmacological lead compounds. For this purpose, single\u2010step analysis of crude venoms has recently been demonstrated using mass spectrometry (MS) techniques. Reproducible profiles of ions in MS and MS\/MS spectra may also be used to compare venoms from different species. In this work matrix\u2010assisted laser desorption\/ionization time\u2010of\u2010flight mass spectrometry (MALDI\u2010TOFMS) was used to obtain mass patterns of the major peptides (&lt;8\u2009kDa) found in pooled venoms from the genera\n                    <jats:italic>Bothrops<\/jats:italic>\n                    and\n                    <jats:italic>Crotalus<\/jats:italic>\n                    . Venoms from five different\n                    <jats:italic>Bothrops<\/jats:italic>\n                    species (\n                    <jats:italic>B. jararaca<\/jats:italic>\n                    ,\n                    <jats:italic>B. insularis<\/jats:italic>\n                    ,\n                    <jats:italic>B. alternatus<\/jats:italic>\n                    ,\n                    <jats:italic>B. jararacussu<\/jats:italic>\n                    , and\n                    <jats:italic>B. neuwiedi<\/jats:italic>\n                    ) and three\n                    <jats:italic>Crotalus<\/jats:italic>\n                    species (\n                    <jats:italic>C. viridis<\/jats:italic>\n                    ,\n                    <jats:italic>C. adamanteus<\/jats:italic>\n                    and\n                    <jats:italic>C. durissus terrificus<\/jats:italic>\n                    ) were analyzed. In agreement with other reports, venoms from\n                    <jats:italic>Bothrops<\/jats:italic>\n                    species contained a variety of peptides in the range\n                    <jats:italic>m\/z<\/jats:italic>\n                    1000\u20131500, and in some samples larger components (\n                    <jats:italic>m\/z<\/jats:italic>\n                    7000\u20138000) were detected. In the\n                    <jats:italic>Crotalus<\/jats:italic>\n                    species venoms were rich in peptides ranging from\n                    <jats:italic>m\/z<\/jats:italic>\n                    1000\u20131500 and 4000\u20135500. MS\/MS experiments on the low molecular mass peptides (\n                    <jats:italic>m\/z<\/jats:italic>\n                    1000\u20131500) confirmed the presence of ten new bradykinin\u2010potentiating peptides among venoms from genera\n                    <jats:italic>Bothrops<\/jats:italic>\n                    and\n                    <jats:italic>Crotalus<\/jats:italic>\n                    . In order to determine whether additional peptides could be identified after partial purification,\n                    <jats:italic>B. jararaca<\/jats:italic>\n                    venom was subjected to size\u2010exclusion chromatography on Sephacryl S\u2010200, and two distinct low molecular mass pools were analyzed further by MALDI\u2010TOFMS. No additional peptides were detected from the pool with masses below 2000\u2009Da but a substantial improvement with better resolution was observed for the pool with masses above 7000\u2009Da, indicating that complex samples such as crude snake venoms can be analyzed for low molecular mass peptides using a single\u2010step procedure. Copyright \u00a9 2005 John Wiley &amp; Sons, Ltd.\n                  <\/jats:p>","DOI":"10.1002\/rcm.1973","type":"journal-article","created":{"date-parts":[[2005,5,24]],"date-time":"2005-05-24T09:17:27Z","timestamp":1116926247000},"page":"1703-1708","source":"Crossref","is-referenced-by-count":64,"title":["Fast analysis of low molecular mass compounds present in snake venom: identification of ten new pyroglutamate\u2010containing peptides"],"prefix":"10.1002","volume":"19","author":[{"given":"Luciana Serr\u00e3o","family":"Wermelinger","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Denis L. S.","family":"Dutra","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana L.","family":"Oliveira\u2010Carvalho","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M\u00e1rcia Regina","family":"Soares","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"suffix":"Jr.","given":"Carlos","family":"Bloch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Russolina B.","family":"Zingali","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2005,5,23]]},"reference":[{"key":"e_1_2_6_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0742-8413(97)00163-1"},{"key":"e_1_2_6_3_2","first-page":"317","volume":"146","author":"St\u00f6ckin R","year":"2000","journal-title":"Methods Mol. 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