ISOLATION AND CHARACTERIZATION OF A HEMORRHAGIN FROM THE VENOM OF CALLOSELASMA-RHODOSTOMA (MALAYAN PIT VIPER)

The major hemorrhagin (termed rhodostoxin) of the venom of Calloselasm a rhodostoma (Malayan pit viper) was purified to electrophoretic homog eneity by Sephadex G-200 gel filtration followed by high performance i on exchange chromatography. The purified hemorrhagin also yielded a si ngle peak in reversed-phase HPLC. It had an isoelectric point of 5.3 a nd a mol. wt of 34,000. Rhodostoxin exhibited potent proteolytic, hemo rrhagic and edema-inducing activities but was not lethal to mice at a dose of 6 mug/g (i.v.). Treatment of rhodostoxin with EDTA eliminated both the proteolytic and hemorrhagic activities completely. The N-term inal sequence of rhodostoxin was determined to be NHEIKRHVDIVVVXDSRFCT K.