{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T07:51:01Z","timestamp":1777535461656,"version":"3.51.4"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1994,11,15]]},"abstract":"<jats:p>Two novel toxins were purified from the venom of the Mexican scorpion Centruroides limpidus limpidus, using an immunoassay based on antibodies raised against noxiustoxin (NTX), a known K(+)-channel-blocker-peptide. The primary structure of C. l. limpidus toxin 1 was obtained by Edman degradation and was shown to be composed of 38 amino acid residues, containing six half-cystines. The first 36 residues of C. l. limpidus toxin 2 were also determined. Both toxins are capable of displacing the binding of radio-labelled NTX to rat brain synaptosomes with high affinity (about 100 pM). These toxins are capable of inhibiting transient K(+)-currents (resembling IA-type currents), in cultured rat cerebellar granule cells. About 50% of the peak currents are reduced by application of a 1.5 microM solution of toxins 1 and 2 The K+ current reduction is partially reversible, under washing but not voltage-dependent. Comparison of the primary structure of C. l. limpidus toxin 1 with other known toxins shows 74% identity with margatoxin, 64% with NTX, 51% with kaliotoxin, 39% with iberiotoxin, 37% with charybdotoxin and Lq2, and 29% with leirutoxin 1. The only invariant amino acids in all these toxins are the six cysteines, a glycine in position 26 and two lysines at positions 28 and 33, respectively. The relevance of these differences in terms of possible structure-function relationships is discussed.<\/jats:p>","DOI":"10.1042\/bj3040051","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:40:39Z","timestamp":1439242839000},"page":"51-56","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":41,"title":["Novel K+-channel-blocking toxins from the venom of the scorpion <i>Centruroides limpidus limpidus<\/i> Karsch"],"prefix":"10.1042","volume":"304","author":[{"given":"B M","family":"Martin","sequence":"first","affiliation":[{"name":"National Institute of Mental Health, Molecular Neurogenetics Unit, Clinical Neuroscience Branch, Building 49 Bl EE1 6, Bethesda, MD 20892, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A N","family":"Ramirez","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica, Instituto de Biotecnolog\u00eda, Universidad Nacional Aut\u00f3noma de M\u00e9xico, Av. Universidad 2001, Apartado Postal 510-3, Cuernavaca, Mor. 62271, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G B","family":"Gurrola","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica, Instituto de Biotecnolog\u00eda, Universidad Nacional Aut\u00f3noma de M\u00e9xico, Av. Universidad 2001, Apartado Postal 510-3, Cuernavaca, Mor. 62271, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M","family":"Nobile","sequence":"additional","affiliation":[{"name":"Instituto di Cibernetica e Biofisica, Via Dodecaneso 33, CNRI-16146 Genova, Italy."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G","family":"Prestipino","sequence":"additional","affiliation":[{"name":"Instituto di Cibernetica e Biofisica, Via Dodecaneso 33, CNRI-16146 Genova, Italy."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"L D","family":"Possani","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica, Instituto de Biotecnolog\u00eda, Universidad Nacional Aut\u00f3noma de M\u00e9xico, Av. Universidad 2001, Apartado Postal 510-3, Cuernavaca, Mor. 62271, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/304\/1\/51\/725488\/bj3040051.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/304\/1\/51\/725488\/bj3040051.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,24]],"date-time":"2021-11-24T00:55:02Z","timestamp":1637715302000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/304\/1\/51\/36567\/Novel-K-channel-blocking-toxins-from-the-venom-of"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1994,11,15]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1994,11,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj3040051","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1994,11,15]]}}}