Novel isoforms of the β and γ subunits of the Xenopus epithelial Na channel provide information about the amiloride binding site and extracellular sodium sensing

Proceedings of the National Academy of Sciences of the United States of America

Volumn 94, Issue 11, 1997, Pages 5949-5954

  Puoti, Alessandro ^a,b   May, Anne ^a   Rossier, Bernard C ^a   Horisberger, Jean Daniel ^a  

^a University of Lausanne Departement de Pharmacologie et de Toxicologie   (Switzerland)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

Aldosterone; Sodium self inhibition; Sodium transport

Indexed keywords

ALDOSTERONE; AMILORIDE;

ALPHA CHAIN; ANIMAL CELL; ARTICLE; BETA CHAIN; BINDING SITE; CHLORIDE CONDUCTANCE; COLON MUCOSA; DRUG RECEPTOR BINDING; ENZYME SUBSTRATE; EPITHELIUM CELL; NONHUMAN; PRIORITY JOURNAL; SODIUM ABSORPTION; SODIUM CURRENT; SODIUM TRANSPORT; XENOPUS;

AMILORIDE; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CELL LINE; DNA PRIMERS; EPITHELIUM; KIDNEY; KINETICS; LUNG; MACROMOLECULAR SUBSTANCES; MOLECULAR SEQUENCE DATA; OOCYTES; ORGAN SPECIFICITY; POLYMERASE CHAIN REACTION; RECOMBINANT FUSION PROTEINS; RNA, COMPLEMENTARY; SODIUM; SODIUM CHANNELS; XENOPUS LAEVIS;

ANIMALIA; XENOPUS LAEVIS;

EID: 0030915273     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.94.11.5949     Document Type: Article

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