Abstracts for Card Indexes
189
Effects of scorpion venom on some physiological processes in cockroach : $AS1RA BABU, K . P . M1JxAL1 K1tISHNA Doss and S . A . T. V1TiKATACI-IARI, Toxicon, 1971, 9, 119 . (Department of Zoology, Sri Venkateswara University, Tirupati, India) . AbedeactThe venom of the scorpion Fieterometrus fulvipes has six protein fractions all of which exhibit cathodic mobility . Soon after injection of 0005 ml of the venom into the cockroach, the heart beat and spiracular movements stopped and the legs show sagging and erratic movements without coordination . Muscle action potentials fail within 10 sec, while those of the nerve cord disappear in 30 to 40 sec. The activities of SDH, LDH and AChE are inhibited to a greater extent in muscle homogenates than in nerve cord homogenates. A gradual drop in oxygen consumption along with a drop in heat production of the cockroach was noted after venom injection .
The release of acid hydrolases from lysosomes by animal venoms : R . ICxAi~x, R. Lai~xECi-rrl3lt and E . KAIS>31t, Toxicon,1971, 9, 125 . (Department of Medical Chemistry, School of Medicine, University of Vienna, Vienna, Austria. A6etrad--The action of three crude venom preparations (V. ammodytes, A.ptsctvorus, Bombina variegate) and of purified venom fractions (melittin from bee venom, direct lytic factor and phospholipase A from cobra venom) upon the lysosomal membrane was investigated by measuring the release of acid hydrolases . All crude venom preparations used release acid hydrolases from lysosomes. Pure fractions from cobra venom (Nr~la ncda L.) exert a relatively weak but significant liberation of acid phospbatase and ß-glucuronidase but not of cathepsin . Mixtures of phospholipase A and direct lytic factor are capable of solubilizing cathepsin, ß-glucuronidase and acid phosphatase from lysosomes . The possible mechanism of this synergistic action is discussed.
Toxicity and some enzymatic properties and activities in the venons of Crotalidae, Elapidae and Viperidae : wALT10t F . KocxoLATY, Enrrx B. LEnnoxn, JOYCE G . DALY and THOMAS A . BILLINGS, Toxicon, 1971, 9, 131 . (Biochemistry Division, U.S . Army Medical Research Laboratory, Fort Knox, Kentucky 40121, U.S .A .) . Abstract-Venons from the Elapidae were found to be the most toxic, followed by the Viperidae and Crotalidae . Venons of the latter showed the highest variation in toxicity among the various species. The Elapidae venoms were practically void of proteolytic activity, while those of the Crotalidae were by far the most potent in this respect with the Viperidae venoms in the intermediate position . Of the three families investigated, the Crotalidae venoms were the richest sources of over-all enzymatic activity .
A comparison of the biological effects of paralytic shellfish poisons from clam, mussel and dinoflagellate : M . H. EvAxs, Toxicon, 1971, 9, 139 . (A .R.C . Institute of Animal Physiology, Babraham, Cambridge, Engiand) . Abslract~axitoxin, the paralytic shellfish poison from the clam 3axfdorrau gtganteus, has been tested on mice, frog sciatic nerves, filaments from the rat cauda equine and the frog sartorius muscle. The effects on all of these preparations were indistinguishable from the effects of paralytic shellfish poisons purified from the mussel Mytüus californtanus and the plankton dinoflagellate Gonyaulax catenel/a. The results of the experiments support the hypothesis that the poisons from all three sources are identical .