Abstract
Phospholipase A2 has been isolated fromthe venom of he Central Asian green toad Bufo viridis in the electroophoretically homogeneous state for the first time by biospecific absorption chromatography. The affinity sorbent used was Affi-Gel 10 with covalently bound phosphatidylserine (PDS). The chemical inertness of the bound PDS to the hydrolytic action of phospholipase A2 and its high tendency to form biospecific complexes have been shown. Some biochemical characteristics of the enzyme isolated have been studied: influence of the pH and of the Ca2+ concentration and dependence of activity on substrate concentration.
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