title: Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes.
abstract: A complementary DNA encoding a voltage-gated chloride channel from Torpedo marmorata electric organ was cloned by expressing hybrid-depleted messenger RNA in Xenopus oocytes. The predicted protein has a sequence of 805 amino acids containing several putative membrane-spanning domains. Expression of the protein in Xenopus oocytes shows that it is sufficient for channel function.
authors.affiliation: Centre for Molecular Neurobiology (ZMNH), Hamburg University, Germany.
authors.forename: T J
authors.initials: TJ
authors.lastname: Jentsch
authors.forename: K
authors.initials: K
authors.lastname: Steinmeyer
authors.forename: G
authors.initials: G
authors.lastname: Schwarz
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002462:Cell Membrane / Q000648:ultrastructure; D018118:Chloride Channels; D002712:Chlorides; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D004553:Electric Conductivity; D015870:Gene Expression; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics* / Q000648:ultrastructure; D008969:Molecular Sequence Data; D009865:Oocytes; D012333:RNA, Messenger / Q000235:genetics; D012995:Solubility; D014982:Xenopus laevis
chemical_list: D018118:Chloride Channels; D002712:Chlorides; D008565:Membrane Proteins; D012333:RNA, Messenger; D004247:DNA