Electrophysiology of Ammonium Transport Proteins
نویسندگان
چکیده
منابع مشابه
Substrate specificity of Rhbg: ammonium and methyl ammonium transport.
Rhbg is a nonerythroid membrane glycoprotein belonging to the Rh antigen family. In the kidney, Rhbg is expressed at the basolateral membrane of intercalated cells of the distal nephron and is involved in NH4+ transport. We investigated the substrate specificity of Rhbg by comparing transport of NH3/NH4+ with that of methyl amine (hydrochloride) (MA/MA+), often used to replace NH3/NH4+, in oocy...
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Introduction Previously we demonstrated in rats that chronic hyperkalemia had no effect on ammonium secretion by the proximal tubule in vivo but that high K+ concentrations inhibited ammonium absorption by the medullary thick ascending limb in vitro. These observations suggested that chronic hyperkalemia may reduce urinary ammonium excretion through effects on medullary transport events. To exa...
متن کاملpH sensitivity of ammonium transport by Rhbg.
Rhbg is a membrane glycoprotein that is involved in NH(3)/NH(4)(+) transport. Several models have been proposed to describe Rhbg, including an electroneutral NH(4)(+)/H(+) exchanger, a uniporter, an NH(4)(+) channel, or even a gas channel. In this study, we characterized the pH sensitivity of Rhbg expressed in Xenopus oocytes. We used two-electrode voltage clamp and ion-selective microelectrode...
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Ammonium transport proteins of the Mep/Amt/Rh family include microbial and plant Mep/Amt members, crucial for ammonium scavenging, and animal Rhesus factors likely involved in ammonium disposal. Recent structural information on two bacterial Mep/Amt proteins has revealed the presence, in the hydrophobic conducting pore, of a pair of preserved histidines proposed to play an important role in sub...
متن کاملInteractions of Quaternary Ammonium Compounds and Proteins
A simple met.hod of titration with a cationic detergent has been developed which permits rapid estimation of the concentration of urinary protein with a minimum of manipulations and time. The method depends on the formation of an insoluble anion-cation complex between quaternary ammonium ions, hereinafter referred to as the cationic detergent, and proteins, in the present instance mainly human ...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2013
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2012.11.402