PARTIAL BIOCHEMICAL-CHARACTERIZATION OF VENOM FROM THE ANT, PSEUDOMYRMEX TRIPLARINUS

Venom from the ant, Pseudomyrmex triplarinus, contains 12 proteins wit h mel. wts of > 100,000-4200, and they constitute 41.5% of the dry wei ght. In comparison with published data on ant, wasp, and bee venoms, w hole venom has intense phospholipase activity and intermediate hemolyt ic activity. Four major proteins were isolated and purified by low pre ssure chromatography. The most abundant protein had a mel. wt of 4200 and weak hemolytic activity. The second most common protein was 20,400 and had phospholipase A, activity. The other two major proteins had m el. wts of 24,500 and 14,100 and both exhibited phospholipase and dire ct hemolytic activities. There are eight minor proteins (>100,000-40,0 00), each present at about 1% or less of the total protein. Assayed as a mixture, they had hyaluronidase activity. Seventeen free amino acid s were detected with aspartic acid, glutamic acid, and proline togethe r making up 72% of the total mass of amino acids. Glycerol was present at a concentration of 3.1% of the dry weight and the venom was devoid of lipids.