420
International Society on Toxinology: European Meeting
P R O T E O L Y T I C A N D C L O T T I N G E N Z Y M E S I N SOME V E N E Z U E L A N S N A K E VENOMS F. GUBEN~EK, V. TURK and B. DRUJAN* Department of Biochemistry, J. Stefan Institute University of Ljubljana, Ljubljana, Yugoslavia and *Instituto Venezolano de Investigaciones Cientificas, Caracas, Venezuela The venoms of Bothrops atrox colombiensis, Bothrops venezuelae and Crotalus vegrandis were studied in order to estimate their content of proteolytic and clotting enzymes. Proteolytic activity toward hemoglobin shows (in all three venoms) two pH optima at pH 5.0 and 8.5. Fibrinogen is degraded only at pH 8"5. The highest fibrinolytic activity was found in the venoms of B. venezuelae and C. vegrandis. Clotting activity was highest in B. venezuelae. It is comparable to the activity of B. asper venom. The venoms of B. atrox colombiensis and C. vegrandis have slightly lower clotting activities. Separation of crude venoms was performed by Sephadex G-100 and DEAE cellulose. Only partial separation of clotting activity was thus achieved. From these preliminary results we conclude that the venoms of the most common Venezuelan snakes, B. atrox colombiensis and B. venezuelae might be useful sources for the isolation of proteinases.
P R O T E I N C O M P L E M E N T A T I O N A N D T H E M O D E OF A C T I O N OF T H E C R O T O X I N C O M P L E X E. HABERMANNand J. SCHAUB Human-Pharmakologisches Institut der Justus-Liebig-Universitaet, Giessen, BRD The interaction between the basic phospholipase As and the acidic crotapotin of the crotoxin complex has been studied. Chemical modifications of the phospholipase As moiety were performed at its amino, histidine and tryptophane groups. The resulting material was tested for degree of substitution, toxicity, phospholipase A activity, and binding to crotapotin. Both phospholipase A activity and basicity are relevant for toxicity. Basicity is also relevant for the interaction with crotapotin.
R E C E N T ASPECTS 1N T H E C H E M I S T R Y A N D B I O C H E M I S T R Y OF A N I M A L VENOMS GERHARD G. HABERMEHL Institute of Organic Chemistry, Technical University, Darmstadt, West Germany Introductory remarks should serve three aspects: Give a review on recent progress, show the present trends and stimulate further progress. Progress has been made during the last 2 yr in the field of chemistry and biochemistry of toxins by quite a number of newly isolated compounds, elucidation of the structures and investigations on their biological meaning. This is especially true for marine chemistry and biochemistry. This field is a very important one, for many other related fields such as clinical aspects of fish poisoning. This again includes pollution problems: many cases of fish poisoning are due to polluted water and it is necessary to know about the naturally occurring toxins to be able to differentiate these symptoms from others due to pollution toxins. Progress has also been made with snake toxins. We know the primary structure of many toxins and in some cases even the three-dimensional structure from X-ray investigations. Many conclusions can be drawn including evolutionary aspects as well as structure/activity relationship. One of the most important aspects is the study of the haemotoxic principles of snake venoms, substances affecting blood clotting. This might be a good example for the other special sessions of this meeting, on practical aspects of venoms. I think that this field will be one of the success-promising ones, as many blood diseases still wait for better treatment. Finally new aspects in the field of amphibian toxins have to be considered. Here, too, quite a number of new compounds have been found, and questions on evolution as well as of medical use and biological aspects have to be solved.