Accession Number : ADA259376


Title :   Single Channel Behavior of a Purified Epithelial Na(+) Channel Subunit that Binds Amiloride


Corporate Author : WALTER REED ARMY INST OF RESEARCH WASHINGTON DC


Personal Author(s) : Sariban-Sohraby, Sarah ; Abramow, Maurice ; Fisher, Richard


Full Text : https://apps.dtic.mil/dtic/tr/fulltext/u2/a259376.pdf


Report Date : Jan 1992


Pagination or Media Count : 8


Abstract : The apical membrane of high electrical resistance epithelia, which is selectively permeable to Na(+), plays an essential role in the maintenance of salt balance. Na(+) entry from the apical fluid into the cells is mediated by amiloride-blockable Na(+)-specific channels. The channel protein purified from both amphibian and mammalian sources, is composed of several subunits, only one of which, the 150-kDa polypeptide, specifically binds the Na(+) transport inhibitor amiloride. The goal of the present study was to investigate whether the isolated amiloride-binding subunit of the channel could conduct Na(+). The patch-clamp techniques was used to study the 150-kDa polypeptide, specifically binds the Na(+) transport inhibitor amiloride. The goal of the present study was to investigate whether the isolated amiloride-binding subunit of the channel could conduct Na(+). The patch-clamp technique was used to study the 150-kDa polypeptide incorporated into a lipid bilayer formed on the tip of a glass pipette. Unitary conductance jumps averaged 4.8 pS at 100 mM Na2HPO4.


Descriptors :   *IONS , *EPITHELIUM , *SODIUM , *CHANNELS , REPRINTS , MEMBRANES(BIOLOGY) , TISSUES(BIOLOGY) , CONDUCTIVITY , PURIFICATION , CHLORIDES , BEEF , CARBOXYL RADICALS , CURRENTS , SALTS , AMIDES , ELECTRICAL RESISTANCE , TRANSPORT , LAYERS , CELLS , PEPTIDES , POLYMERS , LIPIDS , PROTEINS


Subject Categories : Biochemistry
      Anatomy and Physiology
      Inorganic Chemistry
      Organic Chemistry


Distribution Statement : APPROVED FOR PUBLIC RELEASE