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Updated: May 17, 2026
Identification of Hemolytic and Phospholipase Activity in Crude Extracts from Sea Anemones by Straightforward Bioassays
Published on: March 29, 2022
Purification, crystallization and preliminary X-ray diffraction analysis of an acidic phospholipase A2 with
Zhisong Zou1, Fuxing Zeng, Lu Zhang
1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.
Abstract:
Phospholipases A2 (PLA2s) are the major component of snake venoms and exert a variety of relevant toxic actions such as neurotoxicity and myotoxicity, amongst others. An acidic PLA2, here named AhV_aPA, was purified from Agkistrodon halys pallas venom by means of a three-step chromatographic procedure. AhV_aPA migrated as a single band on SDS-PAGE gels, with a molecular weight of about 14 kDa. Like other acidic aPLA2s, AhV_aPA has high enzymatic activity. Tension measurements of mouse thoracic aortic rings remarkably indicated that AhV_aPA could induce a further contractile response on the 60 mM K+-induced contraction, with an EC50 of 369 nmol l(-1). Rod-shaped crystals were obtained by the hanging-drop vapour-diffusion method and diffracted to a resolution limit of 2.30 Å. The crystals belonged to space group P222, with unit-cell parameters a=44.27, b=68.39, c=81.54 Å.
