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An acidic protein with phospholipase A 2 activity was purified to homogeneity from the venom of the Northeast Argentinian viperid Bothrops alternatus by two chromatographic steps: a conventional gel filtration on Sephadex G-75 and reversed phase on C18 HPLC column.A molecular mass of 14185.48Da was determined by mass spectrometry, displaying a homodimer conformation. The kinetic assay demonstrated...
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