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PubMed2001

The effect of external divalent cations on spontaneous non-selective cation channel currents in rabbit portal vein myocytes.

1. The effects of external divalent cations on spontaneous single non-selective cation channel currents were studied in outside-out patches from rabbit portal vein smooth muscle cells in K+-free conditions. 2. In an external medium containing 1.5 mM Ca2+ (Ca2+o) the majority of spontaneous channel currents had a unitary conductance of 23 pS, reversal potential (Vr) of +10 mV and a low open probability (Po) at negative patch potentials. Some channels opened to a lower conductance state of about 13 pS suggesting that the cation channels have two conductance states. Open time and burst duration distributions could both be described by two exponentials with time constants of about of 1 ms and 7 ms for open times and 3 ms and 16 ms for burst durations. 3. In 0 Ca2+o the majority of spontaneous cation channels had a unitary conductance of 13 pS and Vr was shifted to +4 mV. Moreover the longer open time and longer burst duration time constants were both reduced to approximately half the values in 1.5 mM Ca2+o. 4. Compared to 0 Ca2+o the single channel currents in 3 microM and 100 microM Ca2+o had a 5- to 6-fold increase in Po which was accompanied by increases in both open times and burst durations. In 3 microM and 100 microM Ca2+o the unitary conductance of the single channel currents was between 22 and 26 pS. 5. At positive membrane potentials the single channel currents had an increased Po compared to negative potentials which was associated with increased open times and burst durations but these values were similar in 3 microM, 100 microM and 1.5 mM Ca2+o. 6. In 1.5 mM Sr2+o and 1.5 mM Ba2+o channels opened to the higher conductance state of about 22-25 pS and had a 3- to 7-fold greater Po than in 0 Ca2+o. 7. In conclusion, external divalent cations have marked effects on the unitary conductance and kinetic behaviour of non-selective cation channels in rabbit portal vein smooth muscle cells.

Animals↗
PubMed1992

The role of cationized catalase and cationized glucose oxidase in mucosal oxidative damage induced in the rat jejunum.

The successful prevention of hydrogen peroxide-induced damage to the rat jejunal mucosa by cationized catalase is described in this study. Biological damage was induced in a closed circulating intestinal loop of the rat by hydrogen peroxide and by hydroxyl radicals induced in situ via the metal-mediated Haber-Wiess reaction. The mucosal activity of lactate dehydrogenase and the amount of potassium ions were used to quantitatively characterize the tissue damage. Catalase was cationized by reacting it with N,N'-dimethyl-1,3-propanediamine to give a soluble product or with polyhistidine to give an insoluble product. The activity of the modified enzymes was assessed, and their ability to protect the rat jejunal mucosa against oxidative stress was studied. It was found that in all cases the cationized enzymes were superior to the native catalase in their shield capability. A significant protection against Fe(II)/H2O2 and ascorbic acid/copper ion-mediated damage was obtained when the cationized enzymes were used. In the presence of glucose, native glucose oxidase failed to cause damage in the rat jejunal mucosa; however, the cationized enzyme caused profound tissue injury. These findings indicate the potential therapeutic merit of cationized enzymes for the treatment of pathological processes in the intestine, whenever oxidative stress is involved.

Animals↗
PubMed2005

Alkali cation binding and permeation in the rat organic cation transporter rOCT2.

Organic cation transporters of the OCT family mediate downhill transport of organic cations, compatible with carrier, pore, or gate-lumen-gate mechanisms. We studied rat OCT2 expressed in Xenopus oocytes by the two-electrode voltage-clamp technique, including membrane capacitance (C(m)) monitoring. Choline, a transported cationic substrate, elicited the expected inward currents but also elicited decreases of C(m). Similar C(m) decreases were caused by the non-transported inhibitors tetrabutylammonium (a cation) and corticosterone (uncharged). Effects on C(m) were voltage-dependent, with a maximum at -140 mV. These findings suggest that the empty rOCT2 protein can undergo an electrogenic conformation change, with one conformation highly favored at physiological voltage. Moreover, alkali cations elicited considerable inward currents and inhibited uptake of [(14)C]tetraethylammonium with a sequence Cs(+) > Rb(+) > K(+) > Na(+) approximately Li(+). Cs(+) affected current and capacitance with similar affinity (K(0.5) approximately 50 mm). Tetraethylammonium inhibited Cs(+) currents in a concentration-dependent manner. Conversely, Cs(+) inhibited tetraethylammonium uptake by a competitive mechanism. Activation energy of the currents estimated from measurements between 12 degrees C and 32 degrees C was approximately 81 kJ/mol for Cs(+) and 39 kJ/mol for tetramethylammonium, compatible with permeation of Cs(+) through rOCT2 along the same path as organic substrates and by a mechanism different from simple electrodiffusion. Rationalization of Cs(+) selectivity in terms of a pore pointed to a pore diameter of approximately 4 A. Intriguingly, that value matches the known selectivity of rOCT2 for organic compounds. Our data show that selective permeability of rOCT2 is not determined by ligand affinity but might rather be understood in terms of the ion channel concept of a distinct "selectivity filter."

Adrenal Cortex Hormones↗
PubMed1998

Delivery to cancer cells of antisense L-myc oligonucleotides incorporated in fusogenic, cationic-lipid-reconstituted influenza-virus envelopes (cationic virosomes).

Antisense oligodeoxy-nucleoside phosphorothioates (OPTs) of L-myc were encapsulated into reconstituted influenza-virus-A envelopes (virosomes). The envelopes of the virosomes consisted of a single positively charged (cationic) lipid bilayer. Binding of cationic virosomes to cellular receptors that are membrane glycoproteins or glycolipids containing terminal sialic acid is mediated by the hemagglutinin glycoprotein (HA) of the influenza virus. After internalization through receptor-mediated endocytosis, cationic virosomes fuse efficiently with the membranes of the endosomal-cell compartment, and as a consequence the encapsulated OPT are delivered to the cell cytoplasma. Examination by fluorescence microscopy of the cellular uptake of cationic virosomes containing fluorescein-labeled OPT showed rapid and efficient incorporation of virosomes. Addition of cationic virosomes (75-150 microl) containing antisense L-myc OPT in the picomolar range to small-cell-lung-cancer (SCLC) cell cultures that expressed highly the L-myc oncogene led to strong inhibition of thymidine incorporation in a concentration-dependent manner. Virosome-entrapped sense L-myc OPT and random-order OPT had only minimal effects on the thymidine uptake. Cells of SCLC cell line NCI-H82 expressing a very low level of L-myc were not affected by antisense-L-myc virosomes. In Western-blot analysis, expression of L-myc protein was suppressed in the antisense-virosome-treated NCI-H209 cells but not in untreated control NCI-H209 cells. These results suggest that cationic virosomes may have great potential as an efficient delivery system for antisense oligonucleotides in cancer therapy.

Antibodies, Monoclonal↗
PubMed1998

Atomic force microscopy for studying gene transfection mediated by cationic liposomes with a cationic cholesterol derivative.

Atomic force microscopy (AFM) was used for studying gene transfection mediated by cationic liposomes which contain a cationic cholesterol derivative with a different spacer arm. Cationic liposomes were made by a mixture of one of eight cationic cholesterol derivatives and 1,2-dioleoyl-sn-glycero-3-phosphatidyl ethanolamine (DOPE). AFM images showed that vesicles made of the liposome/DNA complex had various diameters depending on each cationic cholesterol derivative with a different spacer arm. The results showed that the diameter of the liposome/DNA complex was well related to the transfection activity of plasmid pSV2CAT DNA to a cultured cell line (NIH3T3). From the results it was found that the vesicles with moderate diameters (from 0.4 to 1.4 microm) were moste effective for gene transfection of plasmid pSV2CAT DNA into the target cell. Neither smaller vesicles (< 400 nm) nor larger vesicles (> 1.4 microm) were adequate for gene transfection. As the gene transfection by the cationic liposomes was mostly inhibited by wortmannin, an inhibitor of endocytosis, it is suggested that the vesicles with moderate diameters were useful for gene transfection by endocytosis.

3T3 Cells↗
PubMed2003

The rearrangement of dicarboranyl methyl cation: a possible synthetic strategy toward cationic closo-tricarbaboranes.

A quantitative study on cationic closo-tricarbaboranes proved their stability and a possible use for them as weakly coordinating ions due to the dispersal of positive charge throughout the cage. The current study explores computationally a synthetic strategy toward their realization in parallel with the benzyl cation-tropylium ion rearrangement. This study shows that cage expansion along with the incorporation of a carbon atom into the cage starting from the dicarboranyl methyl cation is in the realm of the possible. The rearrangements are found to have favorable energy barriers with one transition state. The geometry of the dicarboranyl methyl cations (benzyl cation analogues) with bent CH(2) groups favors the rearrangement into the tropylium analogues. Thus, the comparison of well-known benzyl ion-tropylium ion rearrangement with similar reactions among polyhedral boranes unravels the feasibility of cationic tricarboranes.

Journal Article↗
PubMed2006

Cation-cation interactions in Sr5(UO2)20(UO6)2O16(OH)6(H2O)6 and Cs(UO2)9U3O16(OH)5.

Two novel U6+ compounds, Sr5(UO2)20(UO6)2O16(OH)6(H2O)6 (SrFm) and Cs(UO2)9U3O16(OH)5 (CsFm), have been synthesized by mild hydrothermal reactions. The structures of SrFm (orthorhombic, C2221, a = 11.668(1), b = 21.065 (3), c = 13.273 A, V = 3532.5(1) A3, Z = 2) and CsFm (trigonal, R3c, a = 11.395(2), c = 43.722(7) A, V = 4916.7(1) A3, Z = 6) are rare examples of uranyl compounds that contain cation-cation interactions where an O atom of one uranyl ion is directly linked to another uranyl ion. Both structures are complex frameworks. SrFm contains sheets of polyhedra that are linked through cation-cation interactions with uranyl ions located between the sheets. CsFm possesses an unusually complex framework of vertex- and edge-sharing U6+ polyhedra that incorporates cation-cation interactions.

Journal Article↗
PubMed2004

Cation sensors containing a (bpy)Re(CO)3 group linked to an azacrown ether via an alkenyl or alkynyl spacer: synthesis, characterisation, and complexation with metal cations in solution.

Two [(bpy)Re(CO)3L]+ complexes (bpy = 2,2'-bipyridine), where L contains an aza-15-crown-5 ether which is linked to Re via an alkenyl- or alkynyl-pyridine spacer, have been synthesised along with model complexes. Solutions of the complexes in acetonitrile have been studied by UV-Vis absorption spectroscopy, and by 1D and 2D 1H NMR spectroscopy. Strong UV-Vis bands, assigned to intraligand charge-transfer transitions localised at the L ligands, blue shift on protonation of the azacrown nitrogen atom or on complexation of alkali-metal (Li+, Na+ and K+) or alkaline-earth metal (Mg2+, Ca2+ and Ba2+) cations to the azacrown; the magnitude of the blue shift is dependent on the cation, with protonation giving the largest shift of ca. 100 nm. Cation binding constants in the range of log K= 1-4 depend strongly on the identity of the metal cation. Protonation or cation complexation causes downfield shifts in the 1H NMR resonances from most of the azacrown and L ligand protons, and their magnitudes correlate with those of the blue shifts in the UV-Vis bands; shifts in the azacrown 1H NMR resonances report on how the different metal cations interact with the macrocycle. UV-Vis and 1H NMR spectra of the free L ligands enable the effect of the Re centre to be assessed. Together, the data indicate that the alkene spacer gives a more responsive sensor than the alkyne spacer by providing stronger electronic communication across the L ligand.

Journal Article↗
PubMed2000

Sensing of extracellular cations in CasR-deficient osteoblasts. Evidence for a novel cation-sensing mechanism.

We isolated osteoblastic cell lines from wild-type (CasR(+/+)) and receptor null (CasR(-/-)) mice to investigate whether CasR is present in osteoblasts and accounts for their responses to extracellular cations. Osteoblasts from both CasR(+/+) and CasR(-/-) mice displayed an initial period of cell replication followed by a culture duration-dependent increase in alkaline phosphatase activity, expression of osteocalcin, and mineralization of extracellular matrix. In addition, a panel of extracellular cations, including aluminum and the CasR agonists gadolinium and calcium, stimulated DNA synthesis, activated a transfected serum response element-luciferase reporter construct, and inhibited agonist-induced cAMP in CasR(-/-) osteoblasts. The functional responses to these cations were identical in CasR(+/+) and CasR(-/-) osteoblasts. Thus, the absence of CasR alters neither the maturational profile of isolated osteoblast cultures nor their in vitro responses to extracellular cations. In addition, CasR transcripts could not be detected by reverse transcription-polymerase chain reaction with mouse specific primers in either CasR(+/+) or CasR(-/-) osteoblasts, and immunoblot analysis with a CasR-specific antibody was negative for CasR protein expression in osteoblasts. The presence of a cation-sensing response in osteoblasts from CasR(-/-) mice indicates the existence of a novel osteoblastic extracellular cation-sensing mechanism.

Amino Acid Sequence↗
PubMed1993

Deoxygenation-induced cation fluxes in sickle cells. III. Cation selectivity and response to pH and membrane potential.

Deoxygenation of sickle cells increases membrane permeability to Na, K, and Ca and contributes to cellular cation depletion. This study examines the physiological nature of the pathway that mediates deoxygenation-induced movements of monovalent cations. Deoxygenation-induced Rb influx was a linear function of external Rb concentration, with no evidence of saturation. Activation of the deoxygenation-induced pathway was fostered by alkaline pH (7.5), whereas ion movements via the activated pathway were optimal between pH 6.9 and 7.0 in cells incubated in media in which NO3 replaced Cl to eliminate KCl cotransport. The deoxygenation-induced pathway exhibited no selectivity among the alkali metal cations Li, Na, K, Rb, or Cs, but the monovalent organic cations tetramethylammonium, tetraethylammonium, and N-methylglucamine were excluded. Sickle cells incubated in low-Cl media (external Cl, 40 mM) to depolarize the membrane exhibited increased deoxygenation-induced K efflux and reduced Na influx. Cells treated with valinomycin to hyperpolarize the membrane showed increased deoxygenation-induced Na influx. These characteristics of the deoxygenation-induced transport pathway, linear concentration dependence, lack of cation selectivity, and response to membrane potential, argue against a carrier-mediated mechanism in favor of a diffusional process. The exclusion of small organic cations, however, suggests that factors other than ion size influence deoxygenation-induced permeability.

Anemia, Sickle Cell↗
PubMed1976

The biphasic effect of organic cations on the excretion of other organic cations.

The renal excretion of 14C-choline or 14C-acetylcholine was increased by the infusion of another organic cation at low rates but was decreased by infusion of the same added organic cation at higher rates with the Sperber technique in hens. The range of low rates of infusion was from 1 X 10(-15) to 1 X 10(-8) mol/min. At infusion rates greater than 1 X 10(-8) mol/min, inhibition of tubular excretion was found. At the low infusion rates, thiamine, lysine, quinine, atropine, acetylcholine and methylguanidine were found to increase 14C-choline excretion. The same compounds with the exception of lysine and acetylcholine inhibited 14C-choline excretion at the higher infusion rates. A biphasic effect on 14C-acetylcholine excretion was also observed with added atropine, thiamine and choline over the same infusion range. Increases in 14C-choline excretion occurred during a choline infusion rate that normally produced an excretory tubular maximum for choline whereas increases in 14C-acetylcholine excretion occurred during infusion of tracer amounts of 14C-acetylcholine. The effect of the addition of organic cations was selective for cations since the tubular excretion of organic anions was not affected by the addition of organic cations. The tubular excretion ratio of 14C-thiamine/p-aminohippuric acid increased from 0.25 to 0.95 when the infusion rate of added unlabeled thiamine was increased from 1 X 10(-11) to 1 X 10(-8) mol/min. Enhanced tubular excretion of 14C-thiamine may represent the effect of the increased load of unlabeled thiamine to protect the labeled thiamine from conversion to a nontransportable metabolite. Enhancement of excretion of 14C-choline and 14C-acetyocholine produced by very small amounts of other organic cations may represent either inhibition of tubular reabsorptive transport or induction of tubular excretory transport.

Acetylcholine↗
PubMed1981

Mechanisms of cation permeation across apical cell membrane of Necturus gallbladder: effects of luminal pH and divalent cations on K+ and Na+ permeability.

Conventional microelectrode techniques were combined with unilateral mucosal ionic substitutions to determine the effects of luminal pH and luminal alkali-earth cation concentrations on apical membrane cation permeability in Necturus gallbladder epithelium. Acidification of the mucosal solution caused reversible depolarization of both cell membranes and increase of transepithelial resistance. Low pH media also caused: (a) reduction of the apical membrane depolarization induced by high K, and (b) increase of the apical membrane hyperpolarization produced by Na replacement with Li or N-Methyl-D-glucamine. These results, in conjunction with estimates of cell membrane conductances, indicate that acidification of the luminal solution produces a reduction of apical membrane K permeability (PK). Addition of alkali earth cations (Mg2+, Ca2+, Sr2+, or Ba2+) produced cell membrane depolarization, increase of relative resistance of the luminal membrane and reduction of the apical membrane potential change produced by a high-K mucosal medium. These results, as those produced by low pH, can be explained by a reduction of apical membrane PK. The effects of Ba2+ on membrane potential and relative apical membrane PK were larger than those of all other four cations at all concentrations tested (1-10 mM). The effect of Sr2+ was significantly larger than those of Mg2+ and Ca2+ at 10 mM, but not different at 5 mM. The reduction of PK produced by mucosal acidification appears to be mediated by: (a) nonspecific titration of membrane fixed negative charges, and (b) an effect of luminal proton activity on the apical K channel. Divalent cations reduce apical membrane PK probably by screening negative surface charges. The larger magnitude of the effects of Ba2+ and Sr2+ can be explained by binding to membrane sites, in the surface or in the K channel, in addition to their screening effect. We suggest that the action of luminal pH on K secretion in some segments of the renal tubule could be mediated in part by this pH-dependent K permeability of the luminal membrane.

Animals↗
PubMed2001

High-performance ion-exclusion/cation-exchange chromatography of anions and cations in acid rain waters on a weakly acidic cation-exchange resin.

A new method for the simultaneous determination of anions (sulfate, nitrate, and chloride) and cations (sodium, ammonium, potassium, magnesium, and calcium) in acid rain waters was investigated using high-performance ion-exclusion/cation-exchange chromatography with conductimetric detection on a separation column packed with a polymethacrylate-based weakly acidic cation-exchange resin in the hydrogen-form and an eluent comprising 1.5 mM sulfosalicylic acid-6 mM 18-crown-6 at pH 2.6, operated at 1.5 ml/min. Effective separation and highly sensitive conductimetric detection for the anions and the cations was achieved in about 14 min. Since the ionic balance (equivalents of anions/equivalents of cations) of acid rain waters of different pH (4.40-4.67) ranged from 0.97 to 0.94, evaluation of the water quality of acid rain was possible. This method was successfully applied to the simultaneous determination of the anions and the cations in acid rain transported from mainland China and North Korea to central Japan monitored by a meteorological satellite data analyzer.

Acid Rain↗
PubMed1997

Extracellular divalent cations block a cation non-selective conductance unrelated to calcium channels in rat cardiac muscle.

1. The effect of removing extracellular divalent cations on resting potential (Vrest) and background conductance of rat cardiac muscle was studied. Vrest was measured with 3 M KCl-filled microelectrodes in papillary muscles, or with a patch electrode in ventricular myocytes. Whole-cell membrane currents were measured in myocytes using step or ramp voltage commands. 2. In both muscles and single cells, decrease or removal of Ca2+o and Mg2+o caused a nifedipine-resistant depolarization, which was reversed upon readmission of Ca2+o or Mg2+o (half-maximal effect at 0.8 mM Ca2+o or 3 mM Mg2+o in muscles). 3. In single myocytes, removal of Ca2+o and Mg2+o had no effect on the seal resistance in nonruptured cell-attached recordings, but reversibly induced a current with a reversal potential (Vrev) of -8 +/- 3.4 mV (with internal Cs+; mean +/- S.E.M., n = 23) during whole-cell recordings. The current was insensitive to nifedipine (3-100 microM) or amiloride (1 mM). Vrev was insensitive to changes in the equilibrium potential for chloride ions (ECl). 4. The current induced in the absence of extracellular divalent cations was blocked in a concentration-dependent manner by Ca2+o. (At -80 mV, the affinity constant KCa was 60 microM with a Hill coefficient of 0.9) KCa was voltage dependent at positive but not negative potentials. Mg2+o, Ni2+o, Sr2+o, Ba2+o, Cd2+o and Gd3+o also blocked the current. 5. In 0 mM Na+ (145 mM NMDG+), the inward component of the divalent cation-sensitive current was decreased and Vrev shifted to more negative potentials. 6. These results suggest that a novel conductance pathway, permeable to monovalent cations but not to Cl- and blocked by divalent cations, exists in ventricular myocytes.

Amiloride↗
PubMed1985

Dissociation of the triiodothyronine receptor from the nucleus induced by cations: evidence for divalent cation sensitive and insensitive nuclear sites.

Aliquots of purified rat liver nuclei were diluted at 0 degrees C in isotonic buffers containing monovalent (Na+) or divalent (Ca2, Mg2+) cations. At different times following dilution the nuclear suspensions were centrifuged and the T3 receptor was measured in KCl extracts of the nuclear pellets. The rate of receptor loss after dilution in EDTA was 0.0025 min-1. Dilution in the presence of cations caused a fast release of receptor during the first 10 min. This phase, which was not observed when the nuclei were diluted in EDTA without salt, was followed by a second phase where the receptor was released at the same rate as in EDTA. Receptor release was only dependent on the presence of cations in the dilution buffer during the first 10 min after dilution. The amounts of receptor remaining in the nuclei after the first 10 min of dilution were 51.8 +/- 9.2%, in the presence of Ca2+ and Mg2+, 38.6 +/- 8.9% in 0.15 M NaCl, and 18.0 +/- 4.8% in 0.15 M NaCl in the presence of Ca2+ and Mg2+. The release of receptor was not influenced by the integrity of the nuclear membrane. These results suggest the presence of divalent cation sensitive and insensitive nuclear sites for the T3 receptor, in amounts which could be estimated to be about 48 and 52%, respectively. Other interpretations are also possible, such as the presence of a high proportion of free receptors in the nucleosol, which could be released during the first phase of dilution if the negative charges in chromatin are blocked by cations to avoid redistribution of receptors immediately after dilution.

Animals↗
PubMed2001

Interaction of cations, anions, and weak base quinine with rat renal cation transporter rOCT2 compared with rOCT1.

The rat organic cation transporter (rOCT)-2 was characterized by electrical and tracer flux measurements compared with rOCT1. By applying choline gradients to voltage-clamped Xenopus oocytes expressing rOCT2, potential-dependent currents could be induced in both directions. Tracer flux measurements with seven organic cations revealed similar Michaelis-Menten constant values for both transporters, with the exception of guanidine. In parallel experiments with rOCT2 and rOCT1, inhibition of tetraethylammonium transport by 12 cations, 2 weak bases, corticosterone, and the anions para-amminohippurate, alpha-ketoglutarate, and probenecid was characterized. The IC(50) values of many inhibitors were similar for both transporters, whereas others were significantly different. Mepiperphenidol and O-methylisoprenaline showed an approximately 70-fold lower and corticosterone a 38-fold higher affinity for rOCT2. With the use of these inhibitors together with previous information on cation transporters, experimental protocols are proposed to dissect out the individual contributions of rOCT2 and rOCT1 in intact proximal tubule preparations. Inhibition experiments at different pH levels strongly suggest that the weak base quinine passively permeates the plasma membrane at physiological pH and inhibits rOCT2 from the intracellular side.

Animals↗
PubMed2003

Peptide cation-radicals. A computational study of the competition between peptide N-Calpha bond cleavage and loss of the side chain in the [GlyPhe-NH2 + 2H]+. cation-radical.

Cation-radicals and dications corresponding to hydrogen atom adducts to N-terminus-protonated N(alpha)-glycylphenylalanine amide (Gly-Phe-NH(2)) are studied by combined density functional theory and Møller-Plesset perturbational computations (B3-MP2) as models for electron-capture dissociation of peptide bonds and elimination of side-chain groups in gas-phase peptide ions. Several structures are identified as local energy minima including isomeric aminoketyl cation-radicals, and hydrogen-bonded ion-radicals, and ylid-cation-radical complexes. The hydrogen-bonded complexes are substantially more stable than the classical aminoketyl structures. Dissociations of the peptide N-C(alpha) bonds in aminoketyl cation-radicals are 18-47 kJ mol(-1) exothermic and require low activation energies to produce ion-radical complexes as stable intermediates. Loss of the side-chain benzyl group is calculated to be 44 kJ mol(-1) endothermic and requires 68 kJ mol(-1) activation energy. Rice-Ramsperger-Kassel-Marcus (RRKM) and transition-state theory (TST) calculations of unimolecular rate constants predict fast preferential N-C(alpha) bond cleavage resulting in isomerization to ion-molecule complexes, while dissociation of the C(alpha)bond;CH(2)C(6)H(5) bond is much slower. Because of the very low activation energies, the peptide bond dissociations are predicted to be fast in peptide cation-radicals that have thermal (298 K) energies and thus behave ergodically.

Cations↗
PubMed1993

Kinetical parameters of monovalent cation uptake in yeast calculated on accounting for the mutual interaction of cation uptake and membrane potential.

Kinetical parameters of monovalent cation uptake in yeast are calculated according to a model for mutual interaction of membrane potential and cation uptake. Apparent Km values for monovalent cation uptake obtained from uptake studies are 3-5-times lower than the Km values expected when the membrane potential remains constant at increasing cation concentrations instead of being reduced. The model accounts for various phenomena as (i) the increase in apparent Km of Rb+ uptake accompanying the decrease in maximum rate of uptake found on increasing the cellular K+ content, (ii) the decrease in maximum uptake rate and increase in Km in case of simultaneous transport of phosphate and Rb+, (iii) the change in the maximum uptake rate without a change in Km under conditions that the proton pump is effected and (iv) the absence of an increase in K+ efflux at high depolarizing external cation concentrations.

Cations, Monovalent↗