{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,7]],"date-time":"2026-06-07T16:13:18Z","timestamp":1780848798974,"version":"3.54.1"},"reference-count":63,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2019,11,14]],"date-time":"2019-11-14T00:00:00Z","timestamp":1573689600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["163536\/2013-9"],"award-info":[{"award-number":["163536\/2013-9"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>This work reports the purification and biochemical and functional characterization of ACP-TX-I and ACP-TX-II, two phospholipases A2 (PLA2) from Agkistrodon contortrix pictigaster venom. Both PLA2s were highly purified by a single chromatographic step on a C18 reverse phase HPLC column. Various peptide sequences from these two toxins showed similarity to those of other PLA2 toxins from viperid snake venoms. ACP-TX-I belongs to the catalytically inactive K49 PLA2 class, while ACP-TX-II is a D49 PLA2, and is enzymatically active. ACP-TX-I PLA2 is monomeric, which results in markedly diminished myotoxic and inflammatory activities when compared with dimeric K49 PLA2s, confirming the hypothesis that dimeric structure contributes heavily to the profound myotoxicity of the most active viperid K49 PLA2s. ACP-TX-II exhibits the main pharmacological actions reported for this protein family, including in vivo local myotoxicity, edema-forming activity, and in vitro cytotoxicity. ACP-TX-I PLA2 is cytotoxic to A549 lung carcinoma cells, indicating that cytotoxicity to these tumor cells does not require enzymatic activity.<\/jats:p>","DOI":"10.3390\/toxins11110661","type":"journal-article","created":{"date-parts":[[2019,11,14]],"date-time":"2019-11-14T10:56:34Z","timestamp":1573728994000},"page":"661","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization"],"prefix":"10.3390","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4848-4767","authenticated-orcid":false,"given":"Salom\u00f3n","family":"Huancahuire-Vega","sequence":"first","affiliation":[{"name":"Departamento de Ciencias B\u00e1sicas, Facultad de Ciencias de la Salud, Escuela de Medicina Humana, Universidad Peruana Uni\u00f3n (UPeU), Lima 15, Peru"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luciana M.","family":"Hollanda","sequence":"additional","affiliation":[{"name":"Instituto de Tecnologia e Pesquisa, Universidade Tiradentes (UNIT), Aracaju 49032-490, SE, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mauricio","family":"Gomes-Heleno","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), Campinas 13083-970, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edda E.","family":"Newball-Noriega","sequence":"additional","affiliation":[{"name":"Departamento de Ciencias B\u00e1sicas, Facultad de Ciencias de la Salud, Escuela de Medicina Humana, Universidad Peruana Uni\u00f3n (UPeU), Lima 15, Peru"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergio","family":"Marangoni","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), Campinas 13083-970, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2019,11,14]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1016\/j.toxicon.2003.11.002","article-title":"Excitement ahead: Structure, function and mechanism of snake venom phospholipase A2 enzymes","volume":"42","author":"Kini","year":"2003","journal-title":"Toxicon"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.toxicon.2012.09.006","article-title":"Phospholipases A2: Unveiling the secrets of a functionally versatile group of snake venom toxins","volume":"62","author":"Lomonte","year":"2013","journal-title":"Toxicon"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1246","DOI":"10.1016\/j.bbalip.2006.07.011","article-title":"The phospholipase A2 superfamily and its group numbering system","volume":"1761","author":"Schaloske","year":"2006","journal-title":"Biochim. 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