monensin has been researched along with nonactin* in 6 studies
6 other study(ies) available for monensin and nonactin
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Ionophore-induced Cl- transport in human erythrocyte suspensions: a multinuclear magnetic resonance study.
To investigate the effect of ionophores on Cl- distribution in human erythrocyte suspensions, we measured the membrane potential by using 19F and 31P NMR methods. Incubation of human erythrocytes with 0.005 mM of the neutral ionophores valinomycin and nonactin resulted in membrane potentials of -21.2 and -17.8 mV in the presence and absence of DIDS. However, 0.020 mM of the carboxylic ionophores lasalocid, monensin, and nigericin yielded membrane potentials similar to those measured in the absence of ionophore (-9.4 mV). In methanol, the 35Cl- NMR linewidth in the presence of valinomycin was twice as broad as those observed in the presence of carboxylic ionophores, suggesting that neutral ionophores induce Cl- efflux in part via ion pairing. Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Anti-Bacterial Agents; Chlorides; Erythrocyte Membrane; Erythrocytes; Humans; In Vitro Techniques; Ionophores; Kinetics; Lasalocid; Macrolides; Magnetic Resonance Spectroscopy; Membrane Potentials; Monensin; Nigericin; Valinomycin | 1992 |
Sodium ion-dependent amino acid transport in membrane vesicles of Bacillus stearothermophilus.
Amino acid transport in membrane vesicles of Bacillus stearothermophilus was studied. A relatively high concentration of sodium ions is needed for uptake of L-alanine (Kt = 1.0 mM) and L-leucine (Kt = 0.4 mM). In contrast, the Na(+)-H(+)-L-glutamate transport system has a high affinity for sodium ions (Kt less than 5.5 microM). Lithium ions, but no other cations tested, can replace sodium ions in neutral amino acid transport. The stimulatory effect of monensin on the steady-state accumulation level of these amino acids and the absence of transport in the presence of nonactin indicate that these amino acids are translocated by a Na+ symport mechanism. This is confirmed by the observation that an artificial delta psi and delta mu Na+/F but not a delta pH can act as a driving force for uptake. The transport system for L-alanine is rather specific. L-Serine, but not L-glycine or other amino acids tested, was found to be a competitive inhibitor of L-alanine uptake. On the other hand, the transport carrier for L-leucine also translocates the amino acids L-isoleucine and L-valine. The initial rates of L-glutamate and L-alanine uptake are strongly dependent on the medium pH. The uptake rates of both amino acids are highest at low external pH (5.5 to 6.0) and decline with increasing pH. The pH allosterically affects the L-glutamate and L-alanine transport systems. The maximal rate of L-glutamate uptake (Vmax) is independent of the external pH between pH 5.5 and 8.5, whereas the affinity constant (Kt) increases with increasing pH. A specific transport system for the basic amino acids L-lysine and L-arginine in the membrane vesicles has also been observed. Transport of these amino acids occurs most likely by a uniport mechanism. Topics: Alanine; Allosteric Site; Amino Acids; Anti-Bacterial Agents; Binding, Competitive; Biological Transport; Cell Membrane; Geobacillus stearothermophilus; Glutamates; Glutamic Acid; Hydrogen-Ion Concentration; Ionophores; Kinetics; Leucine; Lysine; Macrolides; Monensin; Sodium | 1991 |
The inhibitory effect of some ionophores on human sperm motility.
The inhibitory effect of five ionophores, namely, A23187, nonactin, nigericin, monensin and m-chlorocarbonyl cyanide phenylhydrazone, on human sperm motility were measured with a trans-membrane migration method. The concentrations of A23187 and nigericin that decreased sperm motility to 50% of control were 20 microM (10.5 mg/l) and 8 microM (5.8 mg/l), respectively. Because these two ionophores were more potent than previously reported membrane-active sperm-immobilizing agents, we propose that ionophores could be a new category of vaginal contraceptive if a pharmaceutical preparation that is safe to be administered in vivo can be developed. Topics: Anti-Bacterial Agents; Calcimycin; Carbonyl Cyanide m-Chlorophenyl Hydrazone; Contraceptive Agents, Female; Humans; Ionophores; Macrolides; Male; Monensin; Nigericin; Sperm Motility | 1986 |
Storage of biogenic amines in guinea-pig brain synaptosomes: influence of proton gradient and membrane potential.
1 The effects of K(+), NaCN and the ionophores monensin, nonactin and carbonyl-cyanide-p-trifluoro-methoxyphenylhydrazone (FCCP) on the contents of [(3)H]-5-hydroxytryptamine ([(3)H]-5-HT), [(3)H]-dopamine and [(3)H]-noradrenaline ([(3)H]-NA) in guinea-pig synaptosomes preloaded with these amines were measured.2 In the presence of Ca(2+), K(+) markedly reduced the amine content of the synaptosomes, indicating an acceleration of spontaneous amine release. In the absence of Ca(2+), K(+) had much less effect.3 Monensin, nonactin and FCCP caused a release of all the three labelled amines. This release was considerably faster and more marked than that induced by K(+) and showed no dependence on Ca(2+). The ionophores did not release lactate-dehydrogenase from synaptosomes.4 NaCN, a blocker of oxidative energy production, did not enhance the spontaneous release of [(3)H]-5-HT nor did it influence the monensin-induced release of [(3)H]-5-HT.5 It is concluded that (a) the intragranular storage of 5-HT, dopamine and NA is dependent on the maintenance of a pH-gradient across the granular membrane as well as on the granular membrane potential; (b) the ionophores cause a non-exocytotic release of granular amines, and (c) blood platelets are partial models for aminergic brain neurones as far as intragranular amine storage is concerned. Topics: Animals; Anti-Bacterial Agents; Biogenic Amines; Brain; Calcium; Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; Guinea Pigs; Hydrogen-Ion Concentration; In Vitro Techniques; L-Lactate Dehydrogenase; Macrolides; Membrane Potentials; Monensin; Potassium; Protons; Synaptosomes | 1983 |
[Determination of several antibiotics using voltamperometry at the interface of nitrobenzene and water].
A new electroanalytical method of voltamperometry at the interface of two immiscible electrolyte solutions (ITIES) is based on electrochemical polarization of a liquid/liquid interface. The resulting current voltage characteristics completely resemble those obtained with metallic electrodes. The charge transfer processes are either the direct ion transfer across the ITIES or the transfer facilitated by macrocyclic ionophores. Determination of tetracycline antibiotics is based on the direct transfer of the cationic forms of these substances in acid media. Determination of valinomycin, nonactin and monensin acting as ion carriers is connected with the facilitated alkali metal ion transfer. In general, antibiotic concentrations higher than 0.02-0.05 mmol/l can be determined with this method. Monensin can also be determined in the extracts of Streptomyces cinnamonensis. Topics: Anti-Bacterial Agents; Electrochemistry; Ion Exchange; Ionophores; Macrolides; Monensin; Nitrobenzenes; Tetracyclines; Valinomycin; Water | 1983 |
Storage of biogenic amines in intact blood platelets of man. Dependence on a proton gradient.
The actions of ionophores with different ion specificities and of thrombin on the release of 14C-labeled 5-hydroxytryptamine, [3H]noradrenaline, and endogenous ATP were measured in human platelets suspended in media with various K+ and Na+ concentrations. Besides thrombin, those ionophores [monensin, nigericin, and the combination of carbonylcyanide-p-trifluoromethoxyphenyl hydrazone (FCCP) with nonactin and/or valinomycin] which cause a rapid collapse of H+ gradients induced a fast and virtually total release of 14C-labeled 5-hydroxytryptamine and [3H]noradrenaline into the various media. FCCP alone, which causes an inversion of the membrane potential to inside negative values, induced a considerably slower amine release. Changes in the K+ and Na+ gradients did not lead to amine release, nor did interference with energy transduction by antimycin A with or without glycolysis inhibitors. Monensin and FCCP did not release ATP, whereas thrombin, added before or after incubation of platelets with FCCP and monensin, caused a marked liberation of the nucleotide. It is concluded that in intact human platelets (a) the intragranular storage of 5-hydroxytryptamine and noradrenaline mainly depends on the proton gradient across the granular membrane, and (b) ionophores causing a collapse of H+ gradients induce non-exocytotic release of 5-hydroxytryptamine and noradrenaline from intracellular storage granules. Topics: Anti-Bacterial Agents; Antimycin A; Biogenic Amines; Blood Platelets; Glycolysis; Humans; In Vitro Techniques; Macrolides; Monensin; Nigericin; Norepinephrine; Potassium; Protons; Serotonin; Sodium | 1982 |