Revised amino acid sequences of the three major phospholipases A 2 from Bungarus fasciatus (banded krait) venom

Abstract

C.-S. Liu, J.-M. Chen, C.-H. Chang, S.-W. Chen, I.-H. Tsai, H.-S. Lu and T.-B. Lo. Revised amino acid sequences of the three major phospholipases A 2 from Bungarus fasciatus (banded krait) venom. Toxicon 28, 1457–1468, 1990.—The structures of three cardiotoxin-like proteins obtained from the venom of Bungarus fasciatus (banded krait) were elucidated previously ( Lu and Lo, 1980, 1981). Since their molecular sizes are similar to that of phospholipase A 2 and since they show weak phospholipase A 2 activities ( Chang et al., 1983), a further study of their primary structures was carried out. Fractions Va, Vb-2 and VI, corresponding to the former V-2, V-3 and VI were determined to be typical phospholipases A 2. Among 118 amino acid residues, they all have in common a Pro 29 between Gly 28 and Gly 30, the latter two residues being implicated in Ca 2+ binding together with Tyr 26 and Asp 47.