THE SEPARATION OF THE ENZYMES AND TOXIC PRINCIPLES OF THE VENOM OF CROTALUS ADAMANTEUS

¹ From the Department of Biochemistry, College of Medicine, University of Cincinnati

1. The ability of the venom of Crotalus adamanteus to destroy cephalin and its ability to digest proteins are due to separate substances in the venom.

2. There has been prepared from the venom an albumose fraction which contains the cephalinase, but is free from proteolytic activity. This fraction is free from heat-coagulable protein, and from the substance which imparts the yellow color to the venom. This fraction cannot be positively identified with any of the compounds or fractions previously isolated from Crotalus venom.

3. A portion of the toxicity of the original venom is retained by the cephalinase fraction, but the toxicity is not parallel to the cephalinase content. This is not in accord with the hypothesis of Belfanti that the toxicity of venoms is due to the lysolecithin and lysocephalin produced by their action.

4. The fraction containing the cephalinase has hemolytic powers of the same order as those of the original venom. This hemolytic activity does not appear to be due to the cephalinase itself, although the venom is capable of producing intensely hemolytic substances by its action on cephalin.

5. Results indicate that the separation of the proteolytic enzymes from cephalinase may be accomplished by adsorption with aluminum hydroxide type C which has been aged eight months.

6. The toxic principles, enzymes and proteins of the venom are all adsorbed by the freshly prepared aluminum hydroxide C.

7. The substance which oxidizes hemoglobin to methemoglobin is different from the proteinase and cephalinase, since it is easily separated from them.