{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T03:29:16Z","timestamp":1767929356571,"version":"3.49.0"},"reference-count":38,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2008,12,31]],"date-time":"2008-12-31T00:00:00Z","timestamp":1230681600000},"content-version":"vor","delay-in-days":6088,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[1992,5]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The complete amino acid sequence of fibrolase, a fibrinolytic enzyme from southern copperhead (<jats:italic>Agkistrodon contortrix contortrix<\/jats:italic>) venom, has been determined. This is the first report of the sequence of a direct\u2010acting, non\u2010hemorrhagic fibrinolytic enzyme found in snake venom. The majority of the sequence was established by automated Edman degradation of overlapping peptides generated by a variety of selective cleavage procedures. The amino\u2010terminus is blocked by a cyclized glutamine (pyroglutamic acid) residue, and the sequence of this region of the molecule was determined by mass spectrometry. Fibrolase is composed of 203 residues in a single polypeptide chain with a molecular weight of 22,891, as determined by the sequence. Its sequence is homologous to the sequence of the hemorrhagic toxin Ht\u2010d of <jats:italic>Crotalus atrox<\/jats:italic> venom and with the sequences of two metalloproteinases from <jats:italic>Trimeresurus flavoviridis<\/jats:italic> venom. Microheterogeneity in the sequence was found at both the amino\u2010terminus and at residues 189 and 192. All six cysteine residues in fibrolase are involved in disulfide bonds. A disulfide bond between cysteine\u2010118 and cysteine\u2010198 has been established and bonds between cysteines\u2010158\/165 and between cysteines\u2010160\/192 are inferred from the homology to Ht\u2010d. Secondary structure prediction reveals a very low percentage of \u03b1\u2010helix (4%), but much greater \u03b2\u2010structure (39.5%). Analysis of the sequence reveals the absence of asparagine\u2010linked glycosylation sites defined by the consensus sequence: asparagine\u2010X\u2010serine\/threonine.<\/jats:p>","DOI":"10.1002\/pro.5560010505","type":"journal-article","created":{"date-parts":[[2009,2,9]],"date-time":"2009-02-09T23:31:38Z","timestamp":1234222298000},"page":"590-600","source":"Crossref","is-referenced-by-count":79,"title":["Amino acid sequence of fibrolase, a direct\u2010acting fibrinolytic enzyme from <i>agkistrodon contortrix contortrix<\/i> venom"],"prefix":"10.1002","volume":"1","author":[{"given":"Anne","family":"Randolph","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Scott H.","family":"Chamberlain","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"H.\u2010L. 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