Energization of sulfate transport in yeast

Sulfate uptake by Saccharomyces cerevisiae is stimulated about 12-fold by preincubation of cells with 1% d-glucose or 1% ethanol. The $\text{K}{}_{\mathrm{<mtext>T</mtext>}}$ remains unchanged (0.34–0.38 mM), the $\text{J}{}_{\mathrm{<mtext>mar</mtext>}}$ increase from 18–20 to 195–230 and 170–185 nmol/min per g dry wt., respectively, after glucose and ethanol preincubation. The stimulation involves protein synthesis (it is suppressed by cycloheximide), has a half-time of 18 min and requires mitochondrial respiration (no or low effect in respiration-deficient mutants and those lacking ADP-ATP transport in mitochondria, as well as after anaerobic preincubation of the wild-type strain, and in low-phosphate cells). The presence of NH₄⁺ and some amino acids (e.g., leucine, aspartate, cysteine and methionine) depressed the stimulation while that of cationic amino acids (typically arginine and lysine) and of K⁺ increased it by 50–80%. The stimulated (i.e., newly synthesized) transport system was degraded with a half-life of about 10 min.     

The role of microfilaments and of microtubules in taurocholate uptake by isolated rat liver cells

The role of microfilaments and microtubules on bile salt transport was studied by investigating the influence of a microfilament and a microtubule inhibitor, cytochalasin B and colchicine, respectively, on taurocholate uptake by isolated hepatocytes in vitro. Hepatocytes were prepared by the enzyme perfusion method and [¹⁴C]taurocholate uptake velocity was determined by a filtration assay. Taurocholate uptake obeyed Michaelis-Menten kinetics, maximal uptake velocity and apparent half-saturation constants averaging $\text{0.87 ±}\text{SD}\text{0.05}\text{nmol}\text{· s}{}^{\mathrm{?1}}\text{· 10}{}^{\mathrm{?6}}\text{cells}$ and $\text{10.9 ± 1.8 μ}\text{M}$, respectively. Cytochalasin B ($\text{4.2–420 μ}\text{M}$) inhibited taurocholate uptake in a competitive fashion; $\text{K}{}_{\mathrm{<mtext>i</mtext>}}$ being $\text{33 ± 7 μ}\text{M}$. At concentrations above 100 μM the compound decreased ³⁶Cl membrane potential and intracellular K⁺ concentration. Other parameters of cell viability were not affected by cytochalasin B. Colchicine (0.1–1.0 mM), by contrast, inhibited taurocholate uptake non-competitively, $\text{K}{}_{\mathrm{<mtext>i</mtext>}}$ being $\text{0.47 ± 0.07}\text{mM}$. The inhibition brought about by colchicine was considerably smaller than that induced by cytochalasin B. None of the parameters of cell viability tested was affected by colchicine. These results suggest that microfilaments may be involved in the carrier-mediated hepatocellular transport of bile salts. This could, at least in part, account for cytochalasin B-induced cholestasis. The contribution of the microtubular system, if any, is less important quantitatively. The mechanisms whereby these two components of the cytoskeleton partake in bile salt transport remain to be elucidated.     

Cotransport of phosphate and sodium by yeast

Phosphate uptake by yeast at pH 7.2 is mediated by two mechanisms, one of which has a $\text{K}{}_{\mathrm{<mtext>m</mtext>}}$ of 30 μM and is independent of sodium, and a sodium-dependent mechanism with a $\text{K}{}_{\mathrm{<mtext>m</mtext>}}$ of 0.6 μM, both $\text{K}{}_{\mathrm{<mtext>m</mtext>}}$ values with respect to monovalent phosphate. The sodium-dependent mechanism has two sites with affinity for Na⁺, with affinity constants of 0.04 and 29 mM. Also lithium enhances phosphate uptake; the affinity constants for lithium are 0.3 and 36 mM. Other alkali ions do not stimulate phosphate uptake at pH 7.2. Rubidium has no effect on the stimulation of phosphate uptake by sodium.Phosphate and arsenate enhance sodium uptake at pH 7.2. The $\text{K}{}_{\mathrm{<mtext>m</mtext>}}$ of this stimulation with regard to monovalent orthophosphate is about equal to that of the sodium-dependent phosphate uptake.The properties of the cation binding sites of the phosphate uptake mechanism and those of the phosphate-dependent cation transport mechanism have been compared. The existence of a separate sodium-phosphate cotransport system is proposed.     

Characterization of the passive and active transport mechanisms for bile acid uptake into rat isolated intestinal epithelial cells

The unstirred water layer has been shown to lead to an underestimation of apparent passive permeability coefficients ($\text{P(}\text{app}\text{)}$) and cause a significant overestimation of apparent $\text{K}{}_{\mathrm{<mtext>m</mtext>}}\text{(K}{}_{\mathrm{<mtext>m</mtext>}}\text{(}\text{app}\text{))}$ values for active transport processes in intestinal whole tissue preparations. Isolated cells offer several potential advantages in the study of transport processes including a decreased diffusion layer of water adjacent to their absorptive membranes. Initial studies in cells isolated from rat intestine involving measurements of CO₂ and lactate production and O₂ consumption showed that overall metabolic pathways were functioning. Next, unidirectional uptake rates of bile acids across the isolated cell membrane were determined following correction for extracellular fluid contamination with a non-absorbable marker. Using epithelial cells isolated from jejunum $\text{P(}\text{app}\text{)}$ for eight bile acid monomers varied from 24.9 (taurocholate) to 1563 (deoxycholate) nmol/min/100 mg protein/mM. From these data the incremental free energy changes for the addition of a hydroxyl, glycine and taurine group to the bile acid molecule were calculated to be 982, 1040 and 1464 cal/mol, respectively, values similar to those obtained after correction for unstirred water layer resistance in whole tissue preparations. Following subtraction of the passive component in isolated ileal cells complete kinetic curves for taurocholate and taurodeoxycholate yielded $\text{V(}\text{app}\text{)}$ values of 109 and 70 nmol/min per 100 mg, respectively. $\text{K}{}_{\mathrm{<mtext>m</mtext>}}\text{(}\text{app}\text{)}$ values of 0.24 mM (taurocholate) and 0.10 mM (taurodeoxycholate) are lower than usually recorded in whole tissue. Bile acid uptake into cells from ileum, but not jejunum, was affected by temperature, metabolic and competitive inhibition. These studies indicate that isolated epithelial cells are a metabolically viable, relatively purified intestinal preparation which discriminates between active and passive transport processes for bile acids under conditions where unstirred water layer artifacts are are minimized.     

Galactose uptake by human platelets in vitro

Galactose transport by human platelets has been studied by measuring the cellular accumulation of the radiolabeled sugar during brief periods of suspension in varying concentrations of galactose. Weighted least-squares regression curves fitted to the measurements (initial velocity versus galactose concentration) indicate that a kinetic model with two saturable components is statistically more consistent with the data than a model based upon a single process ($\text{P < 0.001}$). For the two-component model $\text{K}{}_{\mathrm{<mtext>m</mtext><mtext>1</mtext>}}\text{= 0.29}$ mM, $\text{V}{}_1\text{= 1.2}\text{mmol/min per 10}{}^{15}\text{platelets}$, $\text{K}{}_{\mathrm{<mtext>m</mtext><mtext>2</mtext>}}\text{= 46}\text{mM}$, $\text{V}{}_2\text{= 117}\text{mmol/min per 10}{}^{15}\text{platelets}$. The fact that galactose metabolites did not accumulate during the initial phase of uptake indicates that the uptake process is not mediated by enzymatic catalysis. Surface binding also appears inadequate to explain the uptake. The most likely basis for the kinetic data, therefore, is membrane transport. The kinetics are consistent with transport by coexistent membrane structures as well as with transport by a single structure manifesting negative cooperativity.     

Carnitine movement across muscle cell membranes. Studies in isolated rat muscle

l-Carnitine uptake and exodus was studied in rat extensor digitorum longus muscle in vitro. A saturable transport process was observed, which had an apparent $\text{K}{}_{\mathrm{<mtext>m</mtext>}}$ of 60 μM and $\text{V}$ of 22 nmol/h per g tissue. Transport was inhibited by 2,4-dinitrophenol, sodium azide, anaerobiosis, ouabain, and sodium ion depletion. Analogs of l-carnitine containing a quarternary ammonium group were found to inhibit uptake (d-carnitine, $\text{K}{}_{\mathrm{<mtext>i</mtext>}}\text{= 400 μ}\text{M}$ γ-butyrobetaine, $\text{K}{}_{\mathrm{<mtext>i</mtext>}}\text{= 60 μ}\text{M}$, choline chloride, $\text{K}{}_{\mathrm{<mtext>i</mtext>}}\text{= 14}\text{mM}$), while those not containing this functional group (γ-aminobutyrate, d,l-β-hydroxybutyrate) had no significant effect at concentrations 100 times the apparent $\text{K}{}_{\mathrm{<mtext>m</mtext>}}$ of l-carnitine. Carnitine exodus from rat extensor digitorum longus muscle consisted of two phases. The rapid initial phase was attributed to leakage of l-carnitine from damaged muscle fibers, as it proceeded at nearly the same rate at 0° and 37°C, and leveled off to a rate of near zero after 1 h of incubation in vitro. The quantitatively more important phase of exodus showed a latency of 1–2 h and then proceeded at a linear rate of 40–45 nmol/h per g tissue. The results of this study support the contention that l-carnitine is taken up by a carrier-mediated, active transport system in rat extensor digitorum longus muscle. Functionally, the transport system for uptake is distinct from the process by which carnitine is lost from this muscle.     

Developmental and other characteristics of lysine uptake by rat brain synaptosomes

Synaptosomes isolated from adult or newborn rat cerebrum take up l-lysine by two saturable systems, one with a high affinity low capacity and the other with a low affinity high capacity. Initial rate of uptake for low lysine concentrations is more rapid in newborn, but for high concentrations the rate is greater in adult tissue. Analysis of kinetic data indicates that synaptosomes of the newborn have a higher $\text{V}{}_{\mathrm{<mtext>max</mtext>}}$ than those of the adult for high affinity system but adult synaptosomes have a higher $\text{V}{}_{\mathrm{<mtext>max</mtext>}}$ than newborn for low affinity system. At a physiological lysine concentration of 0.5 mM, the calculated contributions of two systems indicate that the adult uptake occurs for about 71% by low affinity system but the newborn utilizes both systems to the same extent. The uptake is sodium independent but pH dependent. Lysine uptake is inhibited by other dibasic amino acids, arginine and ornithine but not cystine. Kinetic analysis indicates that arginine specifically inhibits the high affinity, low $\text{K}{}_{\mathrm{<mtext>m</mtext>}}$ system for lysine uptake.     

Cockroaches on a treadmill: Aerobic running

Five species of cockroach were tested on a miniature treadmill at three velocities as O₂ consumption () was measured: Gromphadorhina chopardi, Blaberus discoidalis, Eublaberus posticus, Byrsotria fumagata and Periplaneta americana. All cockroaches showed a classical aerobic response to running: increased rapidly from a resting rate to a steady-state on-response varied from under 30 s to 3 min. Recovery after exercise was rapid as well; $\text{t}{}_{\mathrm{<mtext>1</mtext><mtext>2</mtext>}}$ off-response varied from under 30 s to 6 min. These times are faster or similar to mammalian values. varied directly with velocity as in running mammals, birds and reptiles. during steady-state running was only 4–12 times higher than at rest. Running is energetically much less costly per unit time than flying, but the cost of transport per unit distance is much more expensive for pedestrians. The minimal cost of transport (M_run), the lowest necessary to transport a given mass a specific distance, is high in cockroaches due to their small size. The new data suggest that insects may be less economical than comparable sized vertebrates.     

Characterization of valine transport in sea urchin eggs

In unfertilized eggs, the mechanism of valine uptake can be summarized as follows. It is saturable over the external concentration of valine and insensitive to the presence of external sodium, depletion of cellular energy supplies and intracellular acidosis. The activation energy for the transport reaction (16.3 kcal/mol) is within the range of values reported for active transport of small molecules. In fertilized eggs, the total rate of valine uptake can be divided into two components: (i) a Na⁺-insensitive uptake which accounts for about 7% of total absorption as shown by studies in Na⁺-free medium seems to possess the same characteristics as in unfertilized eggs, (ii) a Na⁺-dependent transport of valine which constitutes the main entry is formed about 5 min after fertilization. It follows Michaelis-Menten kinetics characterized by 15-fold increase in $\text{V}{}_{\max }$ with no change in $\text{K}{}_{\mathrm{<mtext>m</mtext>}}$. These two mechanisms have characteristics in common, such as their insensitivity to metabolic energy supply, their energy of activation and their ability to concentrate valine. The relationship between the establishment of the Na⁺-dependent valine uptake and the ionic events triggered by fertilization is discussed.     

Carnitine uptake into human heart cells in culture

The uptake of radiolabeled carnitine and butyrobetaine has been studied in human heart cells (CCL 27). The uptake of carnitine is 3–10-fold higher in heart cells than in fibroblasts ($\text{pmol}\text{· μ}\text{g DNA}{}^{\mathrm{?1}}$). The uptake of carnitine increases with temperature coefficient $\text{K}{}_{\mathrm{<mtext>T</mtext>}}$ of 1.6 in the interval 10–20° C and with a negligible uptake at 4 and 10° C. The uptake of carnitine follows Michaelis-Menten kinetics with a $\text{K}{}_{\mathrm{<mtext>M</mtext>}}$ of $\text{4.8 ± 2.2 μ}\text{M}$ and $\text{V = 8.7 ± 3.2}\text{pmol}\text{· μ}\text{g DNA}{}^{\mathrm{?1}}\text{·}\text{h}{}^{\mathrm{?1}}$. Carnitine uptake is suppressed 90% by NaF (24 mM). Butyrobetaine is taken up into heart cells to the same extent as carnitine with a $\text{K}{}_{\mathrm{<mtext>M</mtext>}}$ of 5.7–17.3 μM and $\text{V = 8.7–9.3}\text{pmol}\text{· μ}\text{g DNA}{}^{\mathrm{?1}}\text{·}\text{h}{}^{\mathrm{?1}}$. Butyrobetaine inhibits competitively the uptake of carnitine and carnitine inhibits the uptake of butyrobetaine to the same extent. No conversion of radiolabeled butyrobetaine to carnitine, or carnitine to methyl choline was observed intra- or extracellulary during incubation. These data are compatible with a selective transport mechanism for carnitine which is also responsible for the uptake of butyrobetaine.     

Slow actions of hyperpolarization on sodium channels in the membrane of myelinated nerve

The mean sodium current, $\text{I}$, and the variance of sodium current fluctuations, var, were measured in myelinated nerve during a depolarization to $\text{V = 40}\text{mV}$ applied from the resting potential ($\text{V}{}_{\mathrm{<mtext>H</mtext>}}\text{= 0}$) or from a hyperpolarizing holding potential $\text{V}{}_{\mathrm{<mtext>H</mtext>}}\text{= ?28}\text{mV}$. From $\text{I}$ and var the relative variations in the number $\text{N}$ and the conductance γ of sodium channels following changes of the holding potential were calculated. Hyperpolarizing the membrane from $\text{V}{}_{\mathrm{<mtext>H</mtext>}}\text{= 0}$ to ?28 mV increased $\text{N}$ by a factor of 3.7, whereas γ decreased by a factor of 0.53. These actions of holding potential on sodium channels develop slowly since 500 ms prepulses to 0 or ?28 mV do not alter the values of $\text{N}$ and γ.     

Thiamine transport in thiamine-deficient rats role of the unstirred water layer

As part or a systematic study of alcoholism and thiamine absorption, the effect of diet-induced thiamine deficiency and the role of the unstirred water layer on thiamine transport were investigated. Using ³H-labeled dextran as a marker of adherent mucosal volume, jejunal uptake of ¹⁴C-labeled thiamine hydrochloride was measured, in vitro, in thiamine-deficient rats and pair-fed controls. Uptake of low thiamine concentrations (0.2 and 0.5 μM) was greater in the thiamine-deficient rats thatn in the controls. In contrast, uptake rates for high thiamine concentrations (20 and 50 μM) were similar in both groups. While $\text{1J}{}_{\max }$ was unaltered, $\text{1K}{}_{\mathrm{m}}$ was decreased in thiamine deficiency, suggesting a decrease in unstirred water layer thickness. Accordingly, the thickness of the water layer was measured in both groups of animals and correlated with $\text{1J}{}_{\max }$ and $\text{1K}{}_{\mathrm{m}}$ under unstirred and st irred conditions. Without stirring, there was no difference in $\text{1J}{}_{\max }$ between the two groups. In contrast, both $\text{1K}{}_{\mathrm{m}}$ and the water layer were reduced in the thiamine-deficient rats. With stirring, $\text{1J}{}_{\max }$ was not affected, but both $\text{1K}{}_{\mathrm{m}}$ and the water layer thickness were reduced to similar values in both groups. Reversal of thiamine deficiency resulted in the return of thiamine uptake and the unstirred water layer thickness to control values. These data support the concept of a dual system of thiamine transport and emphasize the role of the unstirred water layer as an important determinant of transport kinetics not only under physiologic situations but also in diet-induced rat thiamine deficiency, a model for a clinical pathological state. The decrease in the unstirred water layer thickness in thiamine deficiency may be also viewed as a possible adaptive mechanism to facilitate absorption of meager supplies of thiamine.     

Roles of sodium and potassium ions on p-aminohippurate transport in rabbit kidney slices

This investigation was principally undertaken to test the ionic gradient hypothesis as applied to active $\text{p-}\text{aminohippurate}$ uptake in the rabbit kidney cortical slice preparation. Efflux of $\text{p-}\text{aminohippurate}$ from the slice was shown to be independent of external Na⁺ concentration. Transferring slices from a low sodium preincubation to a high sodium incubation medium containing $\text{p-}\text{aminohippurate}$ increased intracellular concentrations of both Na⁺ and K⁺, and $\text{p-}\text{aminohippurate}$ accumulation occurred. Transferring slices from a low sodium preincubation to a high sodium incubation medium containing ouabain and $\text{p-}\text{aminohippurate}$ resulted in a net increase in intracellular Na⁺ concentration but no $\text{p-}\text{aminohippurate}$ accumulation occurred. Different combinations of preincubation and incubation media gave a high to low array of intracellular Na⁺ concentrations and these directly reflected their respective $\text{p-}\text{aminohippurate}$ uptake. These results suggest that the Na⁺-gradient hypothesis does not adequately explain the transport of organic acids in rabbit kidney. These results also suggest that Na⁺ possibly has an intracellular role through its stimulation of $\text{(Na}{}^{\mathrm{+}}\text{+ K}{}^{\mathrm{+}}\text{)-ATPase}$ channeled to energizing the $\text{p-}\text{aminohippurate}$ accumulative mechanism.     

Sodium dependence of maximum flux, JM, and Km of amino acid transport in Ehrlich ascites cells

The Michaelis-Menten parameters, $\text{J}{}_{\mathrm{<mtext>M</mtext>}}$ and $\text{K}{}_{\mathrm{m}}$ of the initial 1-min fluxes of uptake of l-phenylalanine and of α-aminoisobutyric acid were determined for extracellular concentrations of Na⁺ ranging from 0.5 to 110 mequiv/l for Ehrlich ascites tumor cells. The maximal initial flux, $\text{J}{}_{\mathrm{<mtext>M</mtext>}}$, decreased with decrease in extracellular Na⁺ for both α-aminoisobutyric acid and phenylalanine but the $\text{K}{}_{\mathrm{m}}$ for α-aminoisobutyric acid increased markedly as the Na⁺ concentration fell whereas the $\text{K}{}_{\mathrm{m}}$ for phenylalanine decreased. Cycloleucine behaved like phenylalanine.The data provides strong evidence that the Na⁺-independent flux of phenylalanine is an exchange diffusion flux that can be varied by changing the intracellular level of amino acids such as phenylalanine. For phenylalanine, cyclolcucine, and methionine this exchange diffusion flux appears to be additive with the Na⁺-dependent initial flux. α-Aminoisobutyric acid also has an exchange diffusion that is Na⁺-independent but it has a high $\text{K}{}_{\mathrm{m}}$ and is not additive with the Na⁺-dependent flux.     

A chloride requirement for Na+-dependent amino-acid transport by brush border membrane vesicles isolated from the intestine of a mediterranean teleost (Boops salpa)

The uptake of d-glucose, 2-aminoisobutyric acid and glycine was studied with intestinal brush border membrane vesicles of a marine herbivorous fish: Boops salpa. The uptake of these three substances is stimulated by an Na⁺ electrochemical gradient ($\text{C}{}_{\mathrm{<mtext>out</mtext>}}\text{C}{}_{\mathrm{<mtext>in</mtext>}}$). For glucose, an increase of the electrical membrane potential generated by a concentration gradient of the liposoluble anion, SCN^?, increases the Na⁺-dependent transport. This responsiveness to the membrane potential was confirmed by valinomycin. Differently from glucose, uptake of glycine and 2-aminoisobutyric acid requires, besides the Na⁺ gradient, the presence of Cl^? on the external side of the vesicles. In the absence of Cl^?, amino acid uptake is not stimulated by the Na⁺ gradient and is not influenced by an electrical membrane potential generated by SCN^? gradient ($\text{C}{}_{\mathrm{<mtext>out</mtext>}}\text{>C}{}_{\mathrm{<mtext>in</mtext>}}$) or by a K⁺ diffusion potential ($\text{C}{}_{\mathrm{<mtext>in</mtext>}}\text{>C}{}_{\mathrm{<mtext>out</mtext>}}$). This Cl^? requirement differs from the Na⁺ requirement, since a Cl^? gradient ($\text{C}{}_{\mathrm{<mtext>out</mtext>}}\text{>C}{}_{\mathrm{<mtext>in</mtext>}}$) does not result in an accumulation of glycine or 2-aminoisobutyric acid similar to that produced by an Na⁺ gradient.     

Uptake of asialo-glycophorin by the perfused rat liver and isolated hepatocytes

Perfused rat livers took up asialo-glycophorin, a glycoprotein derived from human erythrocyte membraneds, with a $\text{t}{}_{\mathrm{<mtext>1</mtext><mtext>2</mtext>}}$ for the clearance of 7 min. As a comparison, asialo-orosomucoid was taken up by this system with a $\text{t}{}_{\mathrm{<mtext>1</mtext><mtext>2</mtext>}}$ of 3.5 min. Both proteins were digested and their ¹²⁵I labels were released to the perfusate as free ¹²⁵I^?. EGTA completely inhibited uptake of these glycoproteins, but not uptake of denatured bovine serum albumin. Addition of Ca²⁺ reversed the inhibition nearly completely. Isolated hepatocytes had an uptake rate of approximately 3 ng/min per 10⁶ cells for the asialo forms of glycophorin, orosomucoid and fetuin. Cellular uptake of each of these asialoglycoproteins could be inhibited by one of the other proteins. Asialo-fetuin caused a 95% inhibition of the uptake rate of asialo-orosomucoid by the perfused liver. This fetal calf glycoprotein had a similar inhibitory effect on asialo-glycophorin, but only after an initial 40% of the asialo-glycophorin had been taken up by the liver at an almost normal rate during the first 30 min of perfusion. The possiblity of an alternative hepatic removal system for asialo-glycophorin is suggested.     

Errata

The unidirectional uptake into the trophoblast of l-leucine, l-isoleucine, l-phenylalanine, l-tryptophan, l-methionine and l-tyrosine from either the maternal or fetal circulations of an isolated dually-perfused guinea-pig placenta was studied using a single circulation paired-tracer dilution technique. Significant and equal uptakes were found on both sides. l-Phenylalanine uptake kinetics on the fetal side indicated an apparent $\text{K}{}_{\mathrm{<mtext>m</mtext>}}$ of 17.0 mM and a $\text{V}$ of 8.2 μmol/min per g.     

The effects of n-alcohols on sarcoplasmic reticulum vesicles

Short, mild treatments of sarcoplasmic reticulum vesicles with aqueous $\text{n-}\text{alcohols}$ from methanol to $\text{n-}\text{heptanol}$ caused an inhibition of calcium uptake and an enhancement of ATPase activity. The $\text{n-}\text{alcohol}$ treatments increased both calcium-dependent (extra) ATPase activity and calcium-independent (basic) ATPase activity of vesicles. The apparent initial reaction rate of ATPase of $\text{n-}\text{alcohol-treated}$ vesicles was about twice that of control vesicles. With increasing number ($\text{n}$) of carbon atoms of the $\text{n-}\text{alcohols}$, the maximum increment of ATPase activity increased, and both the alcohol concentration ($\text{N}{}_{\mathrm{<mtext>Ca</mtext>}}$) required to inhibit calcium uptake by 50% and the alcohol concentration ($\text{N}{}_{\mathrm{<mtext>ATPase</mtext>}}$) required to enhance ATPase activity by 50% of the maximum increment of ATPase activity decreased as follows.

$\text{N}{}_{\mathrm{<mtext>Ca</mtext>}}\text{=23.5·10}{}^{\mathrm{?0.593n}}\text{M}$

$\text{N}{}_{\mathrm{ATPase}}\text{=35.5·10}{}^{\mathrm{?0.593n}}\text{M}$

The ratio, $\text{N}{}_{\mathrm{<mtext>ATPase</mtext>}}$ to $\text{N}{}_{\mathrm{<mtext>Ca</mtext>}}$, was constant for all $\text{n}$ values. The apparent free energy of binding of the methylene groups of $\text{n-}\text{alcohols}$ to sarcoplasmic reticulum vesicles was evaluated (?796 cal/mole) and compared with data from the partition of $\text{n-}\text{alcohols}$ in octanol and water (?670 cal/mole). The effects of $\text{n-}\text{alcohols}$ on membrane vesicles are discussed on the basis of these data.     

Regulation of diamine oxidase expression by β2-adrenoceptors in normal and hypertrophic rat kidney

The administration of preferential adrenergic receptor antagonists to uninephrectomized rats revealed the $\text{β}{}_2\text{-}\text{adrenergic}$ mediation in diamine oxidase activity increase that occurs in the remaining kidney undergoing compensatory hypertrophy. In fact, $\text{β}{}_1\text{,β}{}_2\text{-}$ or $\text{β}{}_2\text{-}$, but not $\text{α}{}_1\text{-}$, $\text{α}{}_2\text{-}$, or $\text{β}{}_1\text{-}\text{receptor-blocking}$ this enzyme enhancement. Further studies with adrenoceptor agonists, such as epinephrine ($\text{α}{}_1$, $\text{α}{}_2$, $\text{β}{}_1$, $\text{β}{}_2$), isoproterenol ($\text{β}{}_1$, $\text{β}{}_2$) or terbutaline ($\text{β}{}_2$) showed that also in normal rat kidney diamine oxidase activity is under the control of $\text{catecholamine}\text{-β}{}_2\text{-}\text{receptors}$ through a mechanism that involves new synthesis of mRNA and protein. Theophylline, an inhibitor of phosphodiesterase, or forskolin, an activator of adenyl cyclase, increased diamine oxidase activity as does epinephrine or nephrectomy. Thus, catecholamine-triggered $\text{β}{}_2\text{-}\text{receptors}$ coupled to adenyl cyclase are involved in the regulation of diamine oxidase activity in normal and hypertrophic rat kidney.