{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,4]],"date-time":"2026-11-04T16:32:08Z","timestamp":1793809928918,"version":"4.6.1"},"reference-count":31,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2004,4,1]],"date-time":"2004-04-01T00:00:00Z","timestamp":1080777600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[2004,4]]},"abstract":"<jats:p>Phaiodactylipin was purified from the venom of the scorpion <jats:italic>Anuroctonus phaiodactylus<\/jats:italic>. It is the first protein to be purified from a scorpion of the family Iuridae and has a molecular mass of 19\u2003172 atomic mass units. The mature protein is composed of two subunits, the large one consisting of 108 amino acid residues, whereas the small subunit has only 18 residues, and the structure is stabilized by five disulfide bridges. The heterodimer is expressed from a single message containing 769 base pairs and a signal peptide with 16 and\/or 25 amino acid residues. During maturation an internal hexapeptide is excised. There are three putative sites of N\u2010glycosylation, one of which is situated in the small subunit region. The carbohydrate composition of this site was determined by mass spectrometry analysis and was found to contain three hexoses, two N\u2010acetyl\u2010hexoses and two deoxyhexoses. The protein has a calcium dependent phospholipase\u2003A<jats:sub>2<\/jats:sub> type of activity. It is lethal to arthropods (insects and isopods), but not toxic to mammals, using doses up to 20\u2003\u00b5g per 20\u2003g mouse body weight. For crickets, a dose of 5\u2003\u00b5g per animal is lethal; however, when injected into mice it is capable of causing only muscular inflammation, without rupture of the basal membrane of cells. It has a direct hemolytic effect in human erythrocytes and retards the coagulation time of blood. It is an unusual phospholipase\u2003A<jats:sub>2<\/jats:sub>, with only 36% and 50% amino acid sequence identities to the closest known phospholipases, imperatoxin\u2003I and phospholipin, respectively. Identities with bee and Heloderma venom phospholipase are only in the order of 28%.<\/jats:p>","DOI":"10.1111\/j.1432-1033.2004.04047.x","type":"journal-article","created":{"date-parts":[[2004,4,2]],"date-time":"2004-04-02T11:07:39Z","timestamp":1080904059000},"page":"1453-1464","source":"Crossref","is-referenced-by-count":64,"title":["Phaiodactylipin, a glycosylated heterodimeric phospholipase\u2003A<sub>2<\/sub> from the venom of the scorpion <i>Anuroctonus phaiodactylus<\/i>"],"prefix":"10.1111","volume":"271","author":[{"given":"Norma A.","family":"Valdez\u2010Cruz","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cesar V. 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