Abstract
Echis coloratus venom releases bradykinin upon incubation with a kininogn-enriched equine plasma fraction. A procedure is described for the purification of kinin-releasing enzyme from the venom. Two kinin-releasing enzyme preparations were obtained: one, having in addition slight kininase activity, electrophoretically heterogeneous, the other, devoid of kininase activity, electrophoretically homogeneous. The electrophoretically homogeneous enzyme preparation possessed capillary permeability increasing activity, but was devoid of the proteolytic, hemorrhagic and fibrinolytic activities of the venom. This preparation, having an estimated molecular weight of 22,000, hydrolysed arginine and tyrosine esters and synthetic lysine peptides, but not arginine amide nor lysine esters. It was thermostable, sensitive to DFP, insensitive to trasylol and to soybean trypsin inhibitor. The properties of the enzyme are compared with other kallikreins and a possible mode of its action on kininogen is discussed.
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