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PubMed1977

The properties of native and denatured DNA in buoyant rubidium trichloroacetate at neutral pH.

Aqueous RbTCA is generally suitable as a buoyant solvent for both native and denatured DNA at neutral pH and room temperature. Native PM-2 DNA II, for example, is buoyant at 3.29 M salt, 25 degrees C; whereas the denatured strands band together at 4.52 M. Two properties of the solvent make this system uniquely useful for separations based upon the extent of secondary structure. First, the melting transition temperature for chemically unaltered DNA is depressed to room temperature or below. Second, the buoyant density increase accompanying denaturation is extraordinarily large, 174 mg/ml for PM-2 DNA II. This value is three times that found in aqueous NaI and ten times that for CsCl. The properties of the RbTCA buoyant solvent presented here include the compositional and buoyant density gradients and the buoyant density dependence upon base composition. The DNA remains chemically unaltered after exposure to RbTCA as shown by the absence of strand scissions for closed circular DNA and by the unimpaired biological activity in transformation assays. Intact virion DNA may be isolated by direct banding of whole virions in RbTCA gradients without prior phenol extraction. Strongly complexed or covalently bound proteins may be detected by their association with the buoyant polymer in the denaturing density gradient.

Centrifugation, Density Gradient↗
PubMed1980

The early melting of closed duplex DNA: analysis by banding in buoyant neutral rubidium trichloroacetate.

Aqueous RbTCA permits the buoyant banding of both native and denatured DNA at room temperature and neutral pH. A unique property of this solvent is the bouyant resolution of closed circular, underwound DNA (I) from the corresponding nicked (II) species. Conditions are reported here in which PM-2 DNA I is physically resolved from native PM-2 DNA II, the buoyant separation being 1.27 mq/ml in 3.3 M RbTCA at 25 degrees C. The separation between nicked and closed DNAs increases with temperature up to 35.5 degrees C, at which PM-2 DNA II cooperatively melts and subsequently pellets. The isothermal buoyant density of a cloed DNA increases linearly as the linking number (Lk) of the closed DNA decreases. The early melting of closed DNA may be monitored with high precision by buoyant banding in RbTCA, it being possible to detect the disruption of as few as 40 base pairs in PM-2 DNA (10,000 base pairs). The constraint that the linking number be conserved in closed DNA requires that a change in duplex winding be accompanied by a compensating change in supercoiling. We estimate the linking number deficiency of PM-2 DNA I to be 0.094 turns per decibase pair. This result permits the estimation of the EtdBr unwinding angle, phi, by comparison with alternative determinations of the linking number deficiency which depend upom the value of phi. The result obtained here is that phi = 27.7 degrees +/- 0.5 degrees and is approximately independent of temperature over the range 15 degrees-35 degrees.

Centrifugation, Density Gradient↗
PubMed1980

Binding of monovalent cations to Na+,K+-dependent ATPase purified from porcine kidney. I. Simultaneous binding of three sodium and two potassium or rubidium ions to the enzyme.

We previously measured the amounts of Na+ and K+ ions bound to the Na+,K+-dependent ATPase [EC 3.6.1.3] purified from porcine kidney by a modified membrane filtration method [(1979) J. Biochem. 86, 509--523]. In this study, we improved the method for measuring the amount of the active site and measured the amount of Rb+ ions (a K+ congener) bound to the ATPase as well as those of Na+ and K+ ions to get more accurate information on the K+- and Na+-binding sites. The following results were obtained. Two kinds of cation-binding sites were found to exist on the ATPase molecule. One was the Na+-binding sites (3 mol per mol of active site). Na+ ions were bound to the sites cooperatively (Hill coefficient, 2.5--3), and the apparent dissociation constant was 0.20--0.32 mM. Three moles of Na+ ions bound to the sites was displaced by 1 mol of K+ ions bound to the ATPase (phi K, 24 microM). The other was the K+-binding sites (2 mol per mol of active site). Two moles of K+, Rb+, or Na+ ions was bound to the sites cooperatively (Hill coefficient, 1.5--2), and their apparent dissociation constants were 0.044, 0.024, and 2.2 mM, respectively. We measured the amounts of Na+ and Rb+ ions bound to the ATPase in the presence of 0.8 mM NaCl and 0.13 mM RbCl, and obtained unequivocal evidence for the simultaneous binding of 3 mol of Na+ ions and 2 mol of Rb+ ions per mol of active site of the ATPase.

Animals↗
PubMedDate not supplied

Rubidium-82 myocardial uptake and extraction after transient ischemia: PET characteristics.

The effects of transient regional ischemia on monovalent cation uptake and extraction by the myocardium were studied in seven open chest dogs. Following a 10-20% stenosis of the left anterior descending coronary artery to prevent reactive hyperemia, the regional myocardial uptake of the monovalent cation 82Rb (ml/min/g X extraction) was measured before, during, and at 10, 30, and 60-80 min after a 10 min total occlusion of the left anterior descending coronary artery using positron emission tomography. Regional myocardial blood flow was also measured at the same time interval using radiolabeled carbonized microspheres. The regional myocardial extraction of 82Rb was calculated as uptake/flow. In normally perfused myocardial regions there was an inverse relationship between 82Rb extraction and blood flow [extraction = -0.56 (In flow) + 0.46, r = 0.93] over a range of flow from 0.3 to 4 ml/min/g. During the prolonged recovery of 82Rb uptake in the transiently ischemic region, flow had returned to normal levels but 82Rb extraction at a given value of flow was significantly decreased at the 30 and 60-80 min times after release of the occlusion compared with normally perfused regions. Thus, prolonged abnormalities in the 82Rb uptake and extraction occur in myocardium recovering from transient ischemia.

Animals↗
PubMed1988

Lenticular rubidium uptake in hypertensive 'cataract-prone' salt-sensitive rats.

We have previously reported a high incidence of cataract formation in adult hypertensive salt-sensitive rats, suggesting that hypertension may be an important cataractogenic risk factor. Weanling salt-sensitive rats that eventually developed cataracts showed a marked increase in the pressor response to a high-sodium diet compared to salt-sensitive rats that did not develop cataracts. A lens and aqueous fluid electrolyte imbalance occurred in all adult salt-sensitive rats examined, but was greater in the salt-sensitive rats that developed cataracts, suggesting an alteration in lens and/or ciliary ion transport in cataracts associated with hypertension. In the present study, lens 86Rb uptake was measured in adult hypertensive salt-sensitive rats prior to cataract formation. 'Cataract-prone' salt-sensitive hypertensive rats (increased pressor response to a high sodium diet given at weanling age), salt-sensitive hypertensive rats unlikely to develop cataracts and control salt-resistant rats were studied at the age of 16 weeks. Total and ouabain-insensitive lens 86Rb uptake were measured for the determination of ouabain-sensitive uptake, an index of Na+,K+-ATPase activity. Lens ouabain-sensitive 86Rb uptake was low in adult hypertensive cataract-prone salt-sensitive rats before cataract formation compared with values in control resistant rats. Intermediate values were observed in hypertensive salt-sensitive rats unlikely to develop cataracts. These data suggest that altered ion transport may play a pivotal role in cataractogenesis associated with this model of hypertension. The data are also consistent with the concept of a generalized defect in epithelial ion transport, at least in salt-sensitive hypertension.

Animals↗
PubMed1966

A study of rubidium accumulation in Euglena gracillis.

The absorption of Rb(+) by Euglena gracillis var. bacillaris was examined, and an active uptake process could be detected within 1 hour. This was established by experiments that included a time course study and metabolic depression by either reducing the temperature or by addition of 2,4-dinitrophenol. By treating the cells with 0.50 mg/ml chloramphenicol, the rate of glycine incorporation and Rb(+) uptake were inhibited. The possible role of protein synthesis in relation to ion accumulation is discussed.

Eukaryota↗
PubMed1985

Rubidium uptake of mononuclear leukocytes from normotensive and borderline hypertensive first degree relatives to patients with essential hypertension.

Uptake of 86Rubidium of mononuclear leukocytes (MNL) was used as a measure of cellular sodium-potassium pump activity. 86Rb-uptake was determined with the pump stimulated mainly from inside the cells by sodium as well as with a combined stimulation from inside by sodium and from outside by Rb. In the first case there was an increased pump activity in MNL from borderline hypertensive offspring of hypertensive patients (BHO), and this may be related to an increased number of pump sites observed previously (10). Estimation of maximal pump activity (Vmax) of MNL suggested that Vmax of each pump site in MNL from BHO may be decreased compared to control value of MNL from healthy normotensive subjects.

Humans↗
PubMed1986

Regulation and interconversion of the potassium transport systems of Saccharomyces cerevisiae as revealed by rubidium transport.

The kinetics of Rb+ transport in Saccharomyces cerevisiae depended on the K+ content of the cells and on K+ starvation, as follows. In cells with normal K+ (grown at millimolar K+), Rb+ transport was regulated by internal K+. The loss of K+ first decreased the Km and later increased the Vmax of Rb+ transport. K+ starvation of normal-K+ cells for 4-5 h decreased the Km of Rb+ transport below the minimum observed after K+ loss. During this time Eadie-Hofstee plots of Rb+ transport suggest that the existing system was converted into a new one with a higher affinity. Growth at 10 microM K+ only required the system triggered by K+ loss, and the system expressed in K+-starved cells was not expressed under these conditions.

Adenosine Triphosphate↗