Abstract
The cobra venom factor (CVF) from Naja n. siamensis was isolated from crude freeze-dried venom by a combination of ion-exchange chromatography and gel filtration (Bio-Rex 70, Sephadex and QAE-Sephadex). The yield of isolated product was 6–8 mg per g starting material. CVF appeared as a homogenous protein band in polyacrylamide gel electrophoresis with and without SDS present. In equilibrium sedimentation analysis the protein was homogenous with a molecular weight of 133,000. Under reducing conditions three protein bands appeared in polyacrylamide gel electrophoresis in SDS with molecular weights of 71,000, 48,000 and 28,000, corresponding to a total molecular weight of 147,000. All of the bands stained with basic fuchsin, suggesting the presence of carbohydrate. Gel filtration in 6 M quanidine hydrochloride on Sepharose 4B of reduced and alkylated material gave three peaks, each corresponding to one of the bands visible on polyacrylamide gel electrophoresis in SDS. The amino acid composition and N-terminal amino acid sequence of each peak were determined. Using a monospecific antiserum to CVF, molecules immunologically related to CVF were detected in several other elapid venoms.
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