DISSOCIATION OF ENZYMATIC-ACTIVITY FROM TOXIC PROPERTIES OF THE MOST BASIC PHOSPHOLIPASE-A(2) FROM VIPERA-RUSSELLI SNAKE-VENOM BY GUANIDINATION OF LYSINE RESIDUES
As. Babu et Tv. Gowda, DISSOCIATION OF ENZYMATIC-ACTIVITY FROM TOXIC PROPERTIES OF THE MOST BASIC PHOSPHOLIPASE-A(2) FROM VIPERA-RUSSELLI SNAKE-VENOM BY GUANIDINATION OF LYSINE RESIDUES, Toxicon, 32(6), 1994, pp. 749-752
The most basic phospholipase A(2) VRV-PL-VIIIa purified from Russell's
viper venom is a toxic enzyme. It induced neurotoxicity, myotoxicity,
and oedema and was lethal to mice at 5.3 mu g/g body weight. It also
inhibited the coagulation of the human plasma. The epsilon-amino group
s of lysine residues of the toxic enzyme VRV-PL-VIIIa were guanidinate
d with o-methylisourea. Guanidination of the enzyme did not alter the
enzymatic activity markedly. The guanidinated enzyme became non-lethal
in doses up to 16 mu g/g body weight, and failed to elicit neurotoxic
symptoms in experimental animals and oedema in the foot pads of mice.
Also, its myotoxic and anticoagulant potencies were decreased signifi
cantly.