Abstract
Attempts at separation of the various active components of snake venoms have not been very successful. These principles are probably proteins or substances closely related to proteins. 1 They are quite unstable. 1 , 2 For this reason, chemical procedures used in their separation, such as precipitation, extraction or absorption often resulted in the destruction of the less stable elements.
Separation of the hemorrhagic and hemolytic components of moccasin venom by cataphoresis was attempted because it was thought that this procedure might be less destructive. This method had been tried by others without success in an attempt to separate the neurotoxic and coagulant principles of Bothrops venom 3 and the neurotoxin and hemolysin of cobra venom. 4
In the present studies, a cataphoresis chamber was used as described by Todd. 5 An electrical potential of 120 volts D.C. was applied to solutions of moccasin venom for 3 to 5 hours at different hydrogen ion concentrations. The liquids in the anode and cathode chambers were then tested for hemorrhagin and hemolysin.
The hemorrhagin was assayed by using the intradermal venom test in rabbits. 2 It was found that at pH values of 6 and above, the hemorrhagin migrated only to the anode, below pH 4 only to the cathode. Very little migration occurred in the neighborhood of pH 4-5. This indicated that the isoelectric point of the hemorrhagic component of moccasin venom was between pH 4 and 5.
Get full access to this article
View all access options for this article.