Shimoda M, Takagi H, Kurata S, Yoshioka T, Natori S
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
FEBS Lett. 1994 Feb 14;339(1-2):59-62. doi: 10.1016/0014-5793(94)80384-6.
Sapecin is an antibacterial protein of the flesh fly and sapecin B is its homologue structurally similar to charybdotoxin of scorpion venom, which is known to be a K+ channel inhibitor. We found that, like charybdotoxin, sapecin B inhibits part of the voltage pulse-induced K+ currents of rat cerebellar Purkinje cells. We suggest that this effect is due to inhibition of the Ca(+)-activated K+ channel. Probably, sapecin B is a naturally occurring K+ channel inhibitor as well as an antibacterial protein.