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A proteinase, named BmooMPα-I, from the venom of Bothrops moojeni, was purified by DEAE-Sephacel, Sephadex G-75 and heparin-agarose column chromatography. The enzyme was purified to homogeneity as judged by its migration profile in SDS–PAGE stained with coomassie blue, and showed a molecular mass of about 24.5kDa. Its complete cDNA was obtained by RT-PCR and the 615bp codified for a mature protein...
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