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  • 11
    Publication Date: 2019-06-27
    Description: The effects of water immersion on renal bicarbonate and acid excretion were assessed in 10 normal male subjects. Immersion resulted in a highly significant progressive increase in the rate of sodium and bicarbonate excretion, and in urine pH. Immersion was also associated with a significant increase in urine P-CO2; this increase presupposes a maintained rate of hydrogen secretion in the distal tubular segment. The rapidity of onset of the bicarbonaturia (2 hrs of immersion) and the concomitant increase in urinary P-CO2 suggest that enhanced bicarbonate excretion of immersion cannot be completely accounted for by immersion-induced suppression of aldosterone, and that the natriuresis and bicarbonaturia of immersion is mediated in part by an increased proximal rejection of sodium and bicarbonate.
    Keywords: AEROSPACE MEDICINE
    Type: Journal of Laboratory and Clinical Medicine; 84; Dec. 197
    Format: text
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  • 12
    Publication Date: 2019-06-27
    Keywords: AEROSPACE MEDICINE
    Type: Journal of Clinical Endocrinology and Metabolism; 41; Sept
    Format: text
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  • 13
    Publication Date: 2019-06-27
    Description: The present study was undertaken to delineate the effects of water immersion to the neck (NI) on renal plasma flow and glomerular filtration rate as assessed by the clearance of p-aminohippuric acid (PAH) and inulin, respectively. Nine normal male subjects were studied on two occasions, control and NI. The conditions of seated posture and time of day were identical. Immersion did not alter either clearance at a time when sodium excretion was increasing markedly. The constancy of PAH clearance during NI suggests that renal blood flow is unaltered and that the natriuresis of NI is mediated independently of alterations in overall renal perfusion. The sluggish decline of a natriuresis during recovery is consistent with the presence of a humoral factor contributing to the encountered natriuresis.
    Keywords: AEROSPACE MEDICINE
    Type: Journal of Applied Physiology; 41; Aug. 197
    Format: text
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  • 14
    Publication Date: 2019-06-27
    Keywords: AEROSPACE MEDICINE
    Type: Circulation Research; 39; Nov. 197
    Format: text
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  • 15
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 29 (1990), S. 543-547 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A fast Monte Carlo integration algorithm with varying time step is described for cooperative binding of ligands of arbitrary length to a one-dimensional lattice. This algorithm is particularly suitable for strongly cooperative or anticooperative systems, i.e., when the time scales for different kinetic events are very different. As an application, the kinetics of a bimodal two-ligand system are briefly discussed.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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  • 16
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 14 (1975), S. 2401-2415 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Interaction between polylysine and DNA's of varied G + C contents was studied using thermal denaturation and circular dichroism (CD). For each complex there is one melting band at a lower temperature tm, corresponding to the helix-coil transition of free base pairs, and another band at a higher temperature t′m, corresponding to the transition of polylysine-bound base pairs. For free base pairs, with natural DNA's and poly(dA-dT) a linear relation is observed between the tm and the G + C content of the particular DNA used. This is not true with poly(dG)·poly(dC), which has a tm about 20°C lower than the extrapolated value for DNA of 100% G + C. For polylysine-bound base pairs, a linear relation is also observed between the t′m and the G + C content of natural DNA's but neither poly(dA-dT) nor poly(dG)·poly(dC) complexes follow this relationship. The dependence of melting temperature on composition, expressed as dtm/dXG·C, where XG·C is the fraction of G·C pairs, is 60°C for free base pairs and only 21°C for polylysine-bound base pairs. This reduction in compositional dependence of Tm is similar to that observed for pure DNA in high ionic strength. Although the t′m of polylysine-poly(dA-dT) is 9°C lower than the extrapolated value for 0% G + C in EDTA buffer, it is independent of ionic strength in the medium and is equal to the tm0 extrapolated from the linear plot of tm against log Na+. There is also a noticeable similarity in the CD spectra of polylysine· and polyarginine·DNA complexes, except for complexes with poly(dA-dT). The calculated CD spectrum of polylysine-bound poly(dA-dT) is substantially different from that of polyarginine-bound poly(dA-dT).
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 17
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 18 (1979), S. 765-788 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Exact solutions are obtained for the time dependence of the extent of irreversible binding of ligands that cover more than one lattice site to a homogeneous one-dimensional lattice. The binding may be cooperative or noncooperative and the lattice either finite or infinite. Although the form of the solution is most convenient when the ligand concentration is buffered, exact numerical or approximate analytical solutions, including upper and lower bounds, can be derived for the case of variable ligand concentration as well. The physical reason behind the relative simplicity of the kinetics of irreversible as opposed to reversible binding in such systems is discussed.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 18
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 18 (1979), S. 2037-2050 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Many ligands, including basic polypeptides, histones, and other proteins bind nonspecifically to DNA in such a way as to render unavailable for further binding several contiguous sites (generally bases or base pairs). An accurate description of the kinetics of such large ligand binding requires a more complex theoretical analysis than does the study of the binding of small ligands to DNA. An exact analytical solution of the problem does not appear feasible. Instead, a Monte Carlo approach is developed which provides an essentially exact numerical solution by simulating the binding experiment using a model one-dimensional lattice to represent the DNA molecule. For the limiting cases of totally irreversible binding and of instantaneous redistribution of bound ligands along the lattice, relatively simple equations can be written and solved for the binding kinetics. These solutions and their realms of applicability are discussed in some detail.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 19
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 20 (1981), S. 1651-1669 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Approximate methods are developed and evaluated for treating the rate of binding ligands that cover several contiguous sites to a homogeneous one-dimensional lattice, which represents a nucleic acid or other linear biopolymer. The model requires as input only the number of lattice sites necessary for binding, the total number (possibly infinite) of lattice sites, and elementary rate constants for the cooperative and noncooperative association and dissociation of the ligand on the lattice. The computational methods employed are an extension of the triplet closure approximation from the helix-coil (single-site ligand) problem to the large ligand binding problem. It is found that consideration of clusters of n + 2 lattice sites, where each ligand covers n sites, gives a surprisingly accurate description of the kinetics. The approximation is implemented by an extension of the matrix-iteration approach proposed by Craig and Crothers. The effects of the finite lattice length, as well as the capability to treat ligand motion along the lattice, are incorporated. When all symmetries are taken into consideration, the time required for the matrix iteration calculation rises only linearly with the ligand length n and is considerably less than that of the Monte Carlo method, which is used as a standard for comparison.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 20
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 23 (1984), S. 1249-1259 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: We consider the irreversible dissociation kinetics of proteins that bind cooperatively and nonspecifically to DNA. Our model consists of an infinitely long one-dimensional nucleic acid lattice on which are bound protein ligands. A set of adjacent bound proteins forms a cluster of length n. A protein molecule may dissociate from any site within the bound cluster, not only from the ends, as was assumed in a previous model of this process due to Lohman [(1983) Biopolymers 22, 1697-1713]. By considering this additional pathway, we present a more general treatment of the dissociation kinetics of cooperatively bound ligands. We show that dissociation from the (n-2) internal positions of an n-cluster is an important pathway when the initial fractional saturation of the lattice is close to unity and the co operatively is low. When the fractional saturation is initially equal to 1 and the co operatively is low, our model does not give the zero-order dissociation kinetics predicted by the Lohman model.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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