Abstract
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.
Original language | English |
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Pages (from-to) | 59-62 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 339 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 1994 Feb 14 |
Externally published | Yes |
Keywords
- Antibacterial protein
- Charybdotoxin
- K channel inhibitor
- Purkinje cell
- Sapecin B
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology