Characterisation of the biochemical and biological variations from the venom of the death adder species (Acanthophis antarcticus, A-praelongus and A-pyrrhus)
L. Van Der Weyden et al., Characterisation of the biochemical and biological variations from the venom of the death adder species (Acanthophis antarcticus, A-praelongus and A-pyrrhus), TOXICON, 38(12), 2000, pp. 1703-1713
We report on species variation in the venoms of the three species of death
adder; the Common death adder (Acanthophis antarcticus), the Northern death
adder (Acanthophis praelongus) and the Desert death adder (Acanthophis pyr
rhus). The venoms were found to vary in their biochemical (chromatography)
and biological (PLA(2) activity, anticoagulant activity and reactivity with
commercial death adder antivenom) properties. Each species produced signif
icant differences in the profile and distribution of PLA(2) activity, when
whole venom was applied to a cation-exchange Mono-S column. PLA(2) enzymes
were purified from each venom and termed acanthoxin B (from A. praelongus),
acanthoxin C (from A. pyrrhus) and the previously characterised acanthoxin
A (from A. antarcticus). Acanthoxin B and C showed lower enzymatic activit
ies than acanthoxin A (4.0, 13.7 and 23.9 pmol of phospholipid hydrolyzed/m
in/mg protein, respectively). N-terminal sequencing revealed acanthoxin B t
o share highest homology with the numerous PLA(2) isozymes (Pa-12C, Pale; P
a-12A) from the King brown snake (Pseudechis australis) and Acanthin I from
the Common death adder. Similar to acanthoxin A, acanthoxin C showed highe
st homology with Acanthin I/II, and pseudexin A-chain from the Red-bellied
black snake (Pseudechis porphyriacus). Whole venom from A. antarcticus, A.
praelongus and A. pyrrhus each showed weak anticoagulant activity (being ab
le to prolong coagulation of the plasma for 107, 220 and 195 s. respectivel
y). By immunodiffusion, each venom produced precipitation bands against com
mercial death adder antivenom. (C) 2000 Elsevier Science Ltd. All rights re
served.