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XB-ART-22320
J Biol Chem 1993 Aug 05;26822:16458-64.
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Xenoxins, a family of peptides from dorsal gland secretion of Xenopus laevis related to snake venom cytotoxins and neurotoxins.

Kolbe HV , Huber A , Cordier P , Rasmussen UB , Bouchon B , Jaquinod M , Vlasak R , Délot EC , Kreil G .


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Three new, highly similar peptides from the skin secretion of Xenopus laevis have been purified and analyzed by mass spectrometry and Edman degradation. The 66-amino-acid peptides, termed xenoxin-1, -2, and -3, contain 8 cysteines and show similarity to snake venom cytotoxins and short neurotoxins. Assignment of two out of four disulfide bonds suggests a tertiary structure similar to that of cytotoxins and short neurotoxins. A cDNA encoding pre-xenoxin-1 was isolated from a X. laevis skin cDNA library. The nucleotide sequence predicts the synthesis of a precursor with a signal peptide followed by the sequence of the mature peptide. Xenoxin-1 and -2 lack alpha-neurotoxic activity, have apparently no antibacterial activity, are low in general toxicity as tested in mice, and have no effect on blood coagulation as measured in a Factor VIII procoagulant activity test. Potential functions of xenoxins as well as evolutionary aspects are discussed.

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Species referenced: Xenopus laevis