| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8297952 | Biochemical and Biophysical Research Communications | 2011 | 6 Pages |
Abstract
⺠We studied the expression of kurtoxin in Escherichia coli and its structural characterization. ⺠The four disulfide bond pairings of recombinant kurtoxin was characterized. ⺠Recombinant kurtoxin almost completely inhibited the T-type calcium channel currents.
Keywords
KurtoxinIPTGTFARP-HPLCnuclear magnetic resonanceSDS–PAGETrifluoroacetic acidsodium dodecyl sulfate–polyacrylamide gel electrophoresisisopropyl β-d-thiogalactosideNMRScorpion toxincircular dichroismCysteineMatrix-assisted laser desorption/ionization-time of flight mass spectrometryMALDI-TOF MSpolymerase chain reactionPCRDisulfide bondT-type calcium channelreverse-phase high-performance liquid chromatography
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Authors
Chul Won Lee, Young-Jae Eu, Hye Jung Min, Eun-Mi Cho, Jun-Ho Lee, Ha Hyung Kim, Seung-Yeol Nah, Kenton J. Swartz, Jae Il Kim,