FURTHER OBSERVATIONS ON THE PROPERTIES OF THE LETHAL PROTEIN IN CROTALUS ATROX VENOM

Different forms of DEAE-substituted ion exchange media (fibrous and microgranular cellulose and DEAE-Sephadex) produced essentially identical results in the chromatography of venom protein, although altering the experimental conditions resulted in markedly altered elution patterns. CM-cellulose, over a wide pH range was ineffective in resolving protein components. Molecular sieve filtration of the lethal protein indicated that it behaved on Sephadex, Biogel and Sepharose as a very large molecule, with a molecular weight perhaps greater than 300,000. Preliminary examination of this same protein in the ultracentrifuge, however, did not indicate such a large protein. None of the methods described resulted in a protein which upon immunoelectrophoresis, produced a single precipitin band. (Author)