Characterization of Kinins in Wasp Venom

Abstract

In mammals, kinins are formed from inactive protein precursors by the action of specific proteases at or near the site of their action. Wasp and hornet venoms are in interesting contrast to the mammalian system in that they contain free kinins which act immediately upon injection (Jacques and Schachter, 1954; Schachter and Thain, 1954: Holdstock et al., 1957; Mathias and Schachter, 1958; and Bhoola et al., 1961). In Vespa vulgaris a single major and two minor components were resolved on columns of Amberlite (XE-64). All three kinin activities were completely destroyed by chymotrypsin and greatly reduced by trypsin. Bradykinin and kallidin are not inactivated by trypsin and could be distinguished chromatographically from the wasp kinins (Mathias and Schachter, 1958). Hornet venom contains a single, different kinin which is not inactivated by trypsin (Bhoola et al., 1961). Peptides from wasps and hornets have pharmacological actions very similar to bradykinin and kallidin; they contract isolated smooth muscle preparations, lower arterial blood pressure, increase capillary permeability, and cause pain when applied to an exposed blister base on human skin.