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Identification of two toxins from scorpion ( Leiurus quinquestriatus ) venom which block distinct classes of calcium‐activated potassium channel
Author(s) -
Castle Neil A.,
Strong Peter N.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81095-x
Subject(s) - scorpion , venom , potassium channel , potassium , chemistry , calcium , biology , biophysics , biochemistry , organic chemistry
Two polypeptide toxins from scorpion ( Leiurus quinquestriatus ) venom which block distinct classes of calcium‐activated potassium channels have been identified and partially purified. One toxin, at 50–100, blocks apamin‐sensitive potassium fluxes in hepatocytes and inhibits [ 125 I]monoiodoapamin binding. The other, more basic, toxin blocks apamin‐insensitive potassium fluxes in erythrocytes at 200and, to our knowledge, is the first toxin shown to block the erythrocyte calcium‐activated potassium channel with high affinity. The possible co‐identity of this latter toxin with charybdotoxin is discussed.