Proteins in venoms of two wasps, Polistes comanchus navajoe and Vespa orientalis.
1. By means of gel electrophoresis the basic proteins in venoms of Polistes comanchus navajoe and Vespa orientalis were resolved into 6 and 5 proteins respectively, all of molecular weights greater than 15,000. 2. Several proteins appeared to be similar in both venoms. 3. The main component of P. comanchus venom responsible for hemolysis was isolated, and data concerning its thermolability, molecular weight (approximately 26,000) and amino acid composition show that unlike the cytolytic components of bee and ant venoms which are small peptides, the corresponding functional entity of P. comanchus venom (polistin) is a protein having the characteristics of an enzyme.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001514:Bee Venoms / Q000032:analysis*; D002415:Cats; D002417:Cattle; D004285:Dogs; D004912:Erythrocytes / Q000187:drug effects; D006041:Goats; D006168:Guinea Pigs; D006461:Hemolysis / Q000187:drug effects; D006736:Horses; D006358:Hot Temperature; D006801:Humans; D066298:In Vitro Techniques; D007525:Isoelectric Focusing; D051379:Mice; D010740:Phospholipases / Q000032:analysis; D011506:Proteins / Q000032:analysis* / Q000494:pharmacology; D011817:Rabbits; D051381:Rats; D012756:Sheep; D014862:Wasp Venoms / Q000032:analysis* / Q000633:toxicity
D000596:Amino Acids; D001514:Bee Venoms; D011506:Proteins; D014862:Wasp Venoms; D010740:Phospholipases