Abstract
J. J. Fiordalisi and G. A. Grant. Evidence for a fast-exchange conformational process in α-bungarotoxin. Toxicon 31, 767–775, 1993.—Anomalous behavior of the post-synaptic protein neurotoxin, α-bungarotoxin (α-bgt), has been observed during reverse-phase HPLC. Purified samples of this toxin from two distinct sources elute from reverse-phase columns as two separate peaks. The protein species represented by these two peaks are in rapid equilibrium, the relative ratio of which displays a pH dependency with a pK a of approximately 3. This equilibrium does not involve the dimerization or aggregation of the toxin and appears to be relatively unique to α-bungarotoxin in that similar behavior is not displayed by several other available α-neurotoxins. pH-dependent conformational changes have been documented for several α-neurotoxins whose crystal structures have been determined (α-bungarotoxin, α-cobratoxin, and erabutoxin b). One or more of these may account for the observed behavior of α-bungarotoxin on reverse-phase HPLC.
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