TY - JOUR
T1 - Evidence for a fast-exchange conformational process in α-bungarotoxin
AU - Fiordalisi, James J.
AU - Grant, Gregory A.
N1 - Funding Information:
Acknowledgements-We wish to thank ReGtx~ A~-R~~ and the Washington University Protein Chemistry Laboratory for excellent technical assistance. This work was supported by National Institutes of Health Grant NS-28447.
PY - 1993/6
Y1 - 1993/6
N2 - 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 pKa 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.
AB - 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 pKa 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.
UR - http://www.scopus.com/inward/record.url?scp=0027265201&partnerID=8YFLogxK
U2 - 10.1016/0041-0101(93)90382-S
DO - 10.1016/0041-0101(93)90382-S
M3 - Article
C2 - 8342174
AN - SCOPUS:0027265201
VL - 31
SP - 767
EP - 775
JO - Toxicon
JF - Toxicon
SN - 0041-0101
IS - 6
ER -