Isolation and Characterization of Two New Peptides , Mastoparan C and Crabrolin , from the Venom of the European Hornet , Vespu crubro

Two peptides rich in hydrophobic amino acids have and homogenates of various rat tissues. This suggests that a been isolated from venom sacs of the Europehornet, function of mastoparans and melittin is to facilitate phosphoVeSpU CrUbrO. One peptide (P-2) is structurally and lipases of both venom and victims. functionally related to the tetradwapeptide mastoWe now report the isolation and characterization of two paran and has been named mutopman c* Le~u-~snnew peptides mastoparan C and crabrolin from Vespu crabro Leu-Lys-A1a-Leu-Leu-A1a-Val-A1a-Lys-Lys-llevenom sacs. Introduced from Europe about 140 years ago, V. LeuNH2. The other (p-1) is a tridecapeptide with a new crabro occurs in most of the United States east of the Mississequence: Phe-Leu-Pro-Leu-Ile-Leu-Arg-Lys-Ile-Valsippi. Weighing about four times than the honey bee, Thr-A1a-LeuNH2 which we have named crabrolin’ The Apis melliferu, this rather formidable hornet preys on other peptide releases histamine from rat peritoneal mast insects and is not a nuisance to man. cells with a threshold of -2.5 pg/ml(-8 p ~ ) . Crabrolin also facilitates the action of purified phospholipase A2 from different sources, but it is not quite as active as mastoparan. It is clearly less active than mastoparan in lysing erythrocytes, and it does not release amylase The following were purchased venom sacs of the European hornet, V. crabro (Vespa Laboratories, Spring Mills, PA); phospholipase At