Revised amino acid sequences of the three major phospholipases A2 from Bungarus fasciatus (banded krait) venom.
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 A2 and since they show weak phospholipase A2 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 A2. Among 118 amino acid residues, they all have in common a Pro29 between Gly28 and Gly30, the latter two residues being implicated in Ca2+ binding together with Tyr26 and Asp47.
Liu
C S
CS
Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan, R.O.C.
Chen
J M
JM
Chang
C H
CH
Chen
S W
SW
Tsai
I H
IH
Lu
H S
HS
Lo
T B
TB
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D005591:Chemical Fractionation; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004546:Elapid Venoms / Q000737:chemistry*; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010741:Phospholipases A / Q000737:chemistry*; D054467:Phospholipases A2
D000596:Amino Acids; D004546:Elapid Venoms; D010741:Phospholipases A; D054467:Phospholipases A2