title: Mast cell degranulating peptide forms voltage gated and cation-selective channels in lipid bilayers.
abstract: Mast cell degranulating peptide, a toxin of bee venom, is a polypeptide composed of 22 amino acids. Exposure of the asolectin bilayer to the peptide results in the formation of channels that are more permeable to K+ than Cl-. These channels are activated when the voltage of the cis side, to which the peptide is added, is made positive.
authors: Department of Biophysical Engineering, Faculty of Engineering Science, Osaka University, Japan.
authors: T
authors: T
authors: Ide
authors: T
authors: T
authors: Taguchi
authors: T
authors: T
authors: Morita
authors: M
authors: M
authors: Sato
authors: K
authors: K
authors: Ikenaka
authors: S
authors: S
authors: Aimoto
authors: T
authors: T
authors: Kondo
authors: H
authors: H
authors: Hojo
authors: M
authors: M
authors: Kasai
authors: K
authors: K
authors: Mikoshiba
mesh_terms: D001514:Bee Venoms / Q000032:analysis; D004553:Electric Conductivity; D066298:In Vitro Techniques; D007473:Ion Channels / Q000502:physiology*; D008051:Lipid Bilayers; D008407:Mast Cells / Q000502:physiology*; D008564:Membrane Potentials; D010455:Peptides / Q000502:physiology*; D010713:Phosphatidylcholines
chemical_list: D001514:Bee Venoms; D007473:Ion Channels; D008051:Lipid Bilayers; D010455:Peptides; D010713:Phosphatidylcholines; C008331:mast cell degranulating peptide