Abstract
1. Three hemorrhagic toxins (Ac 1-, Ac 2- and Ac,-proteinases) were isolated from the lyophilized venom of Agkistrodon acutus from China using gel filtration on a Sephadex G-75 column, followed by ehromatography on diethylaminoethyl (DEAE)-Sephadex A-50, DEAE-Sephacel and DEAE-cellulose. 2. Homogeneity was established by the formation of a single band in acrylamide gel electrophoresis, isoelectric focusing and sodium dodecyl sulfate (SDS) acrylamide gel electrophoresis. 3. Three hemorrhagic toxins possessed both lethal and proteolytic activities. These activities were inhibited by ethylenediamine tetraacetic acid (EDTA), ethyleneglycol (β-ammoethyi) N, N, N', N'-tetraacetic acid (EGTA), o-phenanthroline or cysteine, but nol by soybean trypsin inhibitor (SBTI), p-chloromercuribenzoate (PCMB) or diisopropyl fluorophosphate (DFP). 4. Molecular weight of hemorrhagic toxins (Ac 1-, Ac 2- and Ac 3-proteinases) were determined to be 24,500, 25,000 and 57,000, respectively. It was found that hemorrhagic toxins have considerable similarity to hemorrhagic toxins isolated by Nikai et al. (1977) and Sugihara et al. (1978, 1979), but Ac 2- and Ac 3-proteinases from China and Taiwan are electrophoretically unrelated.
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