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Bothropstoxin-I (BthTx-I) is a homodimeric Lys49-PLA 2 from the venom of the snake Bothrops jararacussu, which lacks hydrolytic activity against phospholipid substrates, yet permeabilizes membranes by a Ca 2+ -independent mechanism. The interaction of the BthTx-I with model membranes has been studied by intrinsic tryptophan fluorescence emission (ITFE) spectroscopy. Nine separate mutants...
Agkistrodon snake venoms contain a variety of phospholipases (PLA 2 ), some of which are myotoxic. In this study, we used reverse-phase HPLC to purify PLA 2 from the venom of Agkistrodon halys. The enzyme named as AgkTx-II, a basic Asp49 PLA 2 , has a molecular masses of 13,869.05. The amino acid sequence and molecular mass of AgkTx-II was identical to those of an Asp49 basic...
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