IndraLab

Statements


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"Strong Interaction between hH1 and Lqh III."

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"With this study, we intended to evaluate the effect of Lqh III on slow inactivation of hH1 channels, as we found that Lqh III binds to hH1 channels so tightly such that strong depolarizations, which are needed to induce slow inactivation, can not completely dissociate Lqh III from these channels."

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"Compared with the results obtained for the other two toxins and also for the toxin interaction with muI sodium channels (Chen et al. 2000), the interaction between hH1 and Lqh III shows unusual properties."

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"However, the dissociation rate of Lqh III from hH1 channels was much slower than that from muI channels (at +100 mV, tau off = 2,010 vs. 322 ms), suggesting that Lqh III binds to hH1 channels most strongly and the interaction between the hH1 channel and Lqh III is unusual."